On the public citation graph

Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

0 signed · 913 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1016/0009-2614(82)83585-9openalex-snapshot
Dipolar magnetic field effects in NMR spectra of liquids
inferredcites →https://doi.org/10.1016/0022-2836(87)90679-6openalex-snapshot
Structure of ubiquitin refined at 1.8 Å resolution
inferredcites →https://doi.org/10.1021/bi00152a029openalex-snapshot
Characterization of magnetically orientable bilayers in mixtures of dihexanoylphosphatidylcholine and dimyristoylphosphatidylcholine by solid-state NMR
inferredcites →https://doi.org/10.1021/ja00039a049openalex-snapshot
Ultraviolet resonance Raman study on the binding mode of enkephalin to phospholipid membranes
inferredcites →https://doi.org/10.1021/ja00093a072openalex-snapshot
Facile Acquisition and Assignment of Oriented Sample NMR Spectra for Bilayer Surface-Associated Proteins

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4507732openalex-extracted
Restraint Validation of Biomolecular Structures Determined By NMR in the Protein Data Bank
inferred← citeshttps://doi.org/10.1002/0471266949.bmc302openalex-snapshot
Advances in NMR‐Based Characterization of Drug Substances, Impurities, Degradants, and Drug Metabolites
inferred← citeshttps://doi.org/10.1002/1099-0682(200208)2002:8<2121::aid-ejic2121>3.0.co;2-oopenalex-snapshot
Detecting Small Structural Changes in Metalloproteins by the Use of NMR Pseudocontact Shifts
inferred← citeshttps://doi.org/10.1002/1439-7641(20010917)2:8/9<539::aid-cphc539>3.0.co;2-mopenalex-snapshot
Anisotropy of Rotational Diffusion, Dipole-Dipole Cross-Correlated NMR Relaxation and Angles between Bond Vectors in Proteins
inferred← citeshttps://doi.org/10.1002/1521-3757(20020201)114:3<453::aid-ange453>3.0.co;2-qopenalex-snapshot
De-novo-Strukturbestimmung mit NMR-Spektroskopie auf der Basis von dipolaren Restkopplungen
inferred← citeshttps://doi.org/10.1002/1521-3773(20020201)41:3<437::aid-anie437>3.0.co;2-3openalex-snapshot
De Novo Structure Determination from Residual Dipolar Couplings by NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/1873-3468.13688openalex-snapshot
Protein structure determination using a Riemannian approach
inferred← citeshttps://doi.org/10.1002/1873-3468.15050openalex-snapshot
The E 3 ligase HUWE 1 interacts with ubiquitin non‐covalently via key residues in the HECT domain
inferred← citeshttps://doi.org/10.1002/2211-5463.12807openalex-snapshot
Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites
inferred← citeshttps://doi.org/10.1002/9780470027318.a9193openalex-snapshot
Protein Dynamics
inferred← citeshttps://doi.org/10.1002/9780470034590.emrstm0262openalex-snapshot
Liquid Crystalline Samples: Application to Macromolecular Structure Determination
inferred← citeshttps://doi.org/10.1002/9780470034590.emrstm1240openalex-snapshot
Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/9781118482469.ch1openalex-snapshot
Reactive Species
inferred← citeshttps://doi.org/10.1002/9781118681121.ch13openalex-snapshot
Determination of Protein Structure and Dynamics by NMR
inferred← citeshttps://doi.org/10.1002/9781119802280.ch13openalex-snapshot
NMR for Stereochemical Elucidation
inferred← citeshttps://doi.org/10.1002/9781119972006.ch4openalex-snapshot
Measurement of Structural Restraints
inferred← citeshttps://doi.org/10.1002/9783527644506.refsopenalex-snapshot
References
inferred← citeshttps://doi.org/10.1002/9783527645947.ch5openalex-snapshot
NMR Methods for the Determination of Protein–Ligand Interactions
inferred← citeshttps://doi.org/10.1002/9783527664610.ch8openalex-snapshot
Structural Elucidation of Small Organic Molecules Assistedby NMR in Aligned Media
inferred← citeshttps://doi.org/10.1002/advs.202518469openalex-snapshot
Generating Dynamic Structures Through Physics‐Based Sampling of Predicted Inter‐Residue Geometries
inferred← citeshttps://doi.org/10.1002/ange.200351632openalex-snapshot
NMR Spectroscopic Determination of the Solution Structure of a Branched Nucleic Acid from Residual Dipolar Couplings by Using Isotopically Labeled Nucleotides
inferred← citeshttps://doi.org/10.1002/ange.200603213openalex-snapshot
Schnelle Bestimmung hochaufgelöster Proteinstrukturen mit der FastNMR‐Methode
inferred← citeshttps://doi.org/10.1002/ange.200800225openalex-snapshot
Simultaneous Determination of the Conformation and Relative Configuration of Archazolide A by Using Nuclear Overhauser Effects, J Couplings, and Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/ange.200900476openalex-snapshot
Protein Conformational Flexibility from Structure‐Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin
inferred← citeshttps://doi.org/10.1002/ange.200900760openalex-snapshot
Stereochemistry Determination by Powder X‐Ray Diffraction Analysis and NMR Spectroscopy Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/ange.200902398openalex-snapshot
On the Treatment of Conformational Flexibility when Using Residual Dipolar Couplings for Structure Determination
inferred← citeshttps://doi.org/10.1002/ange.200902561openalex-snapshot
Der Einsatz von Relaxationserhöhungen in einer paramagnetischen Umgebung zur Proteinstrukturbestimmung mit NMR‐Spektroskopie
inferred← citeshttps://doi.org/10.1002/ange.200903649openalex-snapshot
Bestimmung der Konformation des Schlüsselintermediats einer enantioselektiven Palladium‐katalysierten allylischen Substitution mithilfe dipolarer Restkopplungen
inferred← citeshttps://doi.org/10.1002/ange.200906147openalex-snapshot
An Efficient Protocol for NMR‐Spectroscopy‐Based Structure Determination of Protein Complexes in Solution
inferred← citeshttps://doi.org/10.1002/ange.201007221openalex-snapshot
An Iminodiacetic Acid Based Lanthanide Binding Tag for Paramagnetic Exchange NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/ange.201100310openalex-snapshot
Structure, Dynamics, and Kinetics of Weak Protein–Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions
inferred← citeshttps://doi.org/10.1002/ange.201101641openalex-snapshot
Using Side‐Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures
inferred← citeshttps://doi.org/10.1002/ange.201101739openalex-snapshot
Structural Discrimination in Small Molecules by Accurate Measurement of Long‐Range Proton–Carbon NMR Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/ange.201101784openalex-snapshot
Residuale chemische Verschiebungsanisotropie (RCSAs) – ein Parameter zur Konfigurationsanalyse kleiner Moleküle
inferred← citeshttps://doi.org/10.1002/ange.201105241openalex-snapshot
Inferential NMR/X‐ray‐Based Structure Determination of a Dibenzo[a,d]cycloheptenone Inhibitor–p38α MAP Kinase Complex in Solution
inferred← citeshttps://doi.org/10.1002/ange.201107626openalex-snapshot
Is Enantiomer Assignment Possible by NMR Spectroscopy Using Residual Dipolar Couplings from Chiral Nonracemic Alignment Media?—A Critical Assessment
inferred← citeshttps://doi.org/10.1002/ange.201807365openalex-snapshot
Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)
inferred← citeshttps://doi.org/10.1002/ange.201911015openalex-snapshot
NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics
inferred← citeshttps://doi.org/10.1002/ange.202000311openalex-snapshot
Bestimmung komplexer kleiner Molekülstrukturen mittels molekularer Ausrichtungssimulation
inferred← citeshttps://doi.org/10.1002/ange.202011081openalex-snapshot
Configurational Analysis by Residual Dipolar Couplings: Critical Assessment of “Structural Noise” from Thermal Vibrations
inferred← citeshttps://doi.org/10.1002/ange.202305120openalex-snapshot
Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/anie.200351632openalex-snapshot
NMR Spectroscopic Determination of the Solution Structure of a Branched Nucleic Acid from Residual Dipolar Couplings by Using Isotopically Labeled Nucleotides
inferred← citeshttps://doi.org/10.1002/anie.200603213openalex-snapshot
Fast High‐Resolution Protein Structure Determination by Using Unassigned NMR Data
inferred← citeshttps://doi.org/10.1002/anie.200800225openalex-snapshot
Simultaneous Determination of the Conformation and Relative Configuration of Archazolide A by Using Nuclear Overhauser Effects, J Couplings, and Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/anie.200900476openalex-snapshot
Protein Conformational Flexibility from Structure‐Free Analysis of NMR Dipolar Couplings: Quantitative and Absolute Determination of Backbone Motion in Ubiquitin
inferred← citeshttps://doi.org/10.1002/anie.200900760openalex-snapshot
Stereochemistry Determination by Powder X‐Ray Diffraction Analysis and NMR Spectroscopy Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/anie.200902398openalex-snapshot
On the Treatment of Conformational Flexibility when Using Residual Dipolar Couplings for Structure Determination
inferred← citeshttps://doi.org/10.1002/anie.200902561openalex-snapshot
Use of Relaxation Enhancements in a Paramagnetic Environment for the Structure Determination of Proteins Using NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/anie.200903649openalex-snapshot
Determination of the Conformation of the Key Intermediate in an Enantioselective Palladium‐Catalyzed Allylic Substitution from Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/anie.200906147openalex-snapshot
An Efficient Protocol for NMR‐Spectroscopy‐Based Structure Determination of Protein Complexes in Solution
inferred← citeshttps://doi.org/10.1002/anie.201007221openalex-snapshot
An Iminodiacetic Acid Based Lanthanide Binding Tag for Paramagnetic Exchange NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/anie.201100310openalex-snapshot
Structure, Dynamics, and Kinetics of Weak Protein–Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions
inferred← citeshttps://doi.org/10.1002/anie.201101641openalex-snapshot
Using Side‐Chain Aromatic Proton Chemical Shifts for a Quantitative Analysis of Protein Structures
inferred← citeshttps://doi.org/10.1002/anie.201101739openalex-snapshot
Structural Discrimination in Small Molecules by Accurate Measurement of Long‐Range Proton–Carbon NMR Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/anie.201101784openalex-snapshot
Residual Chemical Shift Anisotropy (RCSA): A Tool for the Analysis of the Configuration of Small Molecules
inferred← citeshttps://doi.org/10.1002/anie.201105241openalex-snapshot
Inferential NMR/X‐ray‐Based Structure Determination of a Dibenzo[a,d]cycloheptenone Inhibitor–p38α MAP Kinase Complex in Solution
inferred← citeshttps://doi.org/10.1002/anie.201107626openalex-snapshot
Is Enantiomer Assignment Possible by NMR Spectroscopy Using Residual Dipolar Couplings from Chiral Nonracemic Alignment Media?—A Critical Assessment
inferred← citeshttps://doi.org/10.1002/anie.201807365openalex-snapshot
Conformational Ensemble of Disordered Proteins Probed by Solvent Paramagnetic Relaxation Enhancement (sPRE)
inferred← citeshttps://doi.org/10.1002/anie.201811895openalex-snapshot
High Accuracy Protein Structures from Minimal Sparse Paramagnetic Solid‐State NMR Restraints
inferred← citeshttps://doi.org/10.1002/anie.201911015openalex-snapshot
NMR Analysis of Apo Glutamine‐Binding Protein Exposes Challenges in the Study of Interdomain Dynamics
inferred← citeshttps://doi.org/10.1002/anie.202000311openalex-snapshot
Determination of Complex Small‐Molecule Structures Using Molecular Alignment Simulation
inferred← citeshttps://doi.org/10.1002/anie.202011081openalex-snapshot
Configurational Analysis by Residual Dipolar Couplings: Critical Assessment of “Structural Noise” from Thermal Vibrations
inferred← citeshttps://doi.org/10.1002/anie.202305120openalex-snapshot
Elongated Bacterial Pili as a Versatile Alignment Medium for NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/bip.21160openalex-snapshot
The immunosuppressive activity and solution structures of ubiquitin fragments
inferred← citeshttps://doi.org/10.1002/bip.22017openalex-snapshot
Sucrose in aqueous solution revisited, Part 1: Molecular dynamics simulations and direct and indirect dipolar coupling analysis
inferred← citeshttps://doi.org/10.1002/cbic.200500049openalex-snapshot
Altered Specificity in DNA Binding by the lac Repressor: A Mutant lac Headpiece that Mimics the gal Repressor
inferred← citeshttps://doi.org/10.1002/cbic.200500085openalex-snapshot
High‐Resolution Solid‐State NMR Studies on Uniformly [13C,15N]‐Labeled Ubiquitin
inferred← citeshttps://doi.org/10.1002/cbic.200500110openalex-snapshot
Methyl Groups as Probes of Structure and Dynamics in NMR Studies of High‐Molecular‐Weight Proteins
inferred← citeshttps://doi.org/10.1002/cbic.200500277openalex-snapshot
Effect of the Solvent on the Conformation of a Depsipeptide: NMR‐Derived Solution Structure of Hormaomycin in DMSO from Residual Dipolar Couplings in a Novel DMSO‐Compatible Alignment Medium
inferred← citeshttps://doi.org/10.1002/cbic.200700600openalex-snapshot
Exchange Rate Constants of Invisible Protons in Proteins Determined by NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/cbic.201300193openalex-snapshot
The Dynamics of Lysozyme from Bacteriophage Lambda in Solution Probed by NMR and MD Simulations
inferred← citeshttps://doi.org/10.1002/cbic.201402585openalex-snapshot
Conformation of Inhibitor‐Free HIV‐1 Protease Derived from NMR Spectroscopy in a Weakly Oriented Solution
inferred← citeshttps://doi.org/10.1002/cbic.202400508openalex-snapshot
Ubiquitin's Conformational Heterogeneity as Discerned by Nuclear Magnetic Resonance Spectroscopy
inferred← citeshttps://doi.org/10.1002/ceur.202500074openalex-snapshot
Anisotropic Nuclear Magnetic Resonance Spectroscopy and Density Functional Theory Methodologies Combine with CASE‐3D Analysis for Unambiguous Diastereomeric Differentiation of AMG 176 Macrocycles
inferred← citeshttps://doi.org/10.1002/ceur.202500336openalex-snapshot
Mutations Alter Conformations and Dynamics of APP‐TMDs: An RDC Analysis
inferred← citeshttps://doi.org/10.1002/chem.200902287openalex-snapshot
Enhancing the Orienting Properties of Poly(γ‐benzyl‐ L ‐glutamate) by means of Additives
inferred← citeshttps://doi.org/10.1002/chem.200903378openalex-snapshot
Residual Dipolar Couplings (RDCs) Analysis of Small Molecules Made Easy: Fast and Tuneable Alignment by Reversible Compression/Relaxation of Reusable PMMA Gels
inferred← citeshttps://doi.org/10.1002/chem.201101385openalex-snapshot
Residual Dipolar Coupling Enhanced NMR Spectroscopy and Chiroptics: A Powerful Combination for the Complete Elucidation of Symmetrical Small Molecules
inferred← citeshttps://doi.org/10.1002/chem.201104078openalex-snapshot
Relative and Absolute Configuration of Vatiparol (1 mg): A Novel Anti‐inflammatory Polyphenol
inferred← citeshttps://doi.org/10.1002/chem.201202509openalex-snapshot
Conformational Analysis of the Anti‐obesity Drug Lorcaserin in Water: How To Take Advantage of Long‐Range Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/chem.201406274openalex-snapshot
Generation of Pseudocontact Shifts in Proteins with Lanthanides Using Small “Clickable” Nitrilotriacetic Acid and Iminodiacetic Acid Tags
inferred← citeshttps://doi.org/10.1002/chem.201501842openalex-snapshot
Exploring the Conformational Space of Bridge‐Substituted Dithienylcyclopentenes
inferred← citeshttps://doi.org/10.1002/chem.201701738openalex-snapshot
Microsecond Dynamics in Ubiquitin Probed by Solid‐State 15N NMR Spectroscopy R1ρ Relaxation Experiments under Fast MAS (60–110 kHz)
inferred← citeshttps://doi.org/10.1002/chem.201702126openalex-snapshot
Biphasic Liquid Crystal and the Simultaneous Measurement of Isotropic and Anisotropic Parameters by Spatially Resolved NMR Spectroscopy
inferred← citeshttps://doi.org/10.1002/chem.201704541openalex-snapshot
New Stretching Method for Aligning Gels: Its Application to the Measurement Residual Chemical Shift Anisotropies (RCSAs) without the Need for Isotropic Shift Correction
inferred← citeshttps://doi.org/10.1002/chem.201802800openalex-snapshot
Configurational Analysis by Residual Dipolar Coupling Driven Floating Chirality Distance Geometry Calculations
inferred← citeshttps://doi.org/10.1002/chem.201803912openalex-snapshot
Protein Glycosylation through Sulfur Fluoride Exchange (SuFEx) Chemistry: The Key Role of a Fluorosulfate Thiolactoside
inferred← citeshttps://doi.org/10.1002/chem.202002642openalex-snapshot
Determination of Configuration and Conformation of a Reserpine Derivative with Seven Stereogenic Centers Using Molecular Dynamics with RDC‐Derived Tensorial Constraints**
inferred← citeshttps://doi.org/10.1002/chem.202103559openalex-snapshot
Pushing the Limits of Characterising a Weak Halogen Bond in Solution
inferred← citeshttps://doi.org/10.1002/chem.202303796openalex-snapshot
Is Simultaneous Binding to DNA and Gyrase Important for the Antibacterial Activity of Cystobactamids?
inferred← citeshttps://doi.org/10.1002/chir.23065openalex-snapshot
Configurational analysis by residual dipolar couplings: A critical assessment of diastereomeric differentiabilities
inferred← citeshttps://doi.org/10.1002/cmr.1012openalex-snapshot
Residual dipolar couplings in protein NMR
inferred← citeshttps://doi.org/10.1002/cmr.a.20016openalex-snapshot
Concepts and tools for NMR restraint analysis and validation
inferred← citeshttps://doi.org/10.1002/cmr.a.20020openalex-snapshot
Weakly aligned biological macromolecules in dilute aqueous liquid crystals
inferred← citeshttps://doi.org/10.1002/cmtd.202500011openalex-snapshot
Deuterium NMR in Chiral Polymer‐Based Bimesophasic Lyotropic Mixtures: From the Demixing Process to Analytical Applications
inferred← citeshttps://doi.org/10.1002/cphc.200301041openalex-snapshot
Determination of Chemical Shift Anisotropy Tensors of Carbonyl Nuclei in Proteins through Cross‐Correlated Relaxation in NMR
inferred← citeshttps://doi.org/10.1002/cphc.200700353openalex-snapshot
Simultaneous Definition of High Resolution Protein Structure and Backbone Conformational Dynamics using NMR Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/cphc.201100365openalex-snapshot
Long‐Lived States to Monitor Protein Unfolding by Proton NMR
inferred← citeshttps://doi.org/10.1002/cphc.202000789openalex-snapshot
Using Cross‐Correlated Spin Relaxation to Characterize Backbone Dihedral Angle Distributions of Flexible Protein Segments
inferred← citeshttps://doi.org/10.1002/cphc.202100187openalex-snapshot
Conformational Space Sampled by Domain Reorientation of Linear Diubiquitin Reflected in Its Binding Mode for Target Proteins
inferred← citeshttps://doi.org/10.1002/cphc.202400068openalex-snapshot
Multinuclear Residual Quadrupolar Couplings for Structure and Assignment
inferred← citeshttps://doi.org/10.1002/cplu.202100507openalex-snapshot
Poly(arylisocyanides) as Versatile, Enantiodiscriminating Alignment Media for Small Molecules
inferred← citeshttps://doi.org/10.1002/ejic.202200597openalex-snapshot
Ruthenium Complexes of Rigid, Dianionic, Tetradentate N‐Donor Ligands and their Potential as Catalysts for Water Oxidation
inferred← citeshttps://doi.org/10.1002/ejoc.201500941openalex-snapshot
Determination of the Relative Configuration of β‐Amino Acid Esters Based on Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/ejoc.201801306openalex-snapshot
l ‐Valine Derivatised 1,3,5‐Benzene‐Tricarboxamides as Building Blocks for a New Supramolecular Organogel‐Like Alignment Medium
inferred← citeshttps://doi.org/10.1002/gch2.202300022openalex-snapshot
Spatial Layouts of Low‐Entropy Hydration Shells Guide Protein Binding
inferred← citeshttps://doi.org/10.1002/ijch.201900126openalex-snapshot
Solution NMR Structural Studies of Glycans
inferred← citeshttps://doi.org/10.1002/jcc.21105openalex-snapshot
Performance of density functional models to reproduce observed 13Cα chemical shifts of proteins in solution
inferred← citeshttps://doi.org/10.1002/jcc.24323openalex-snapshot
A simple graphical approach to predict local residue conformation using NMR chemical shifts and density functional theory
inferred← citeshttps://doi.org/10.1002/jcc.26556openalex-snapshot
Exploring the quality of protein structural models from a Bayesian perspective
inferred← citeshttps://doi.org/10.1002/mrc.1837openalex-snapshot
Inter-domain orientation and motions in VAT-N explored by residual dipolar couplings and15N backbone relaxation
inferred← citeshttps://doi.org/10.1002/mrc.1963openalex-snapshot
SESAME‐HSQC for simultaneous measurement of NH and CH scalar and residual dipolar couplings
inferred← citeshttps://doi.org/10.1002/mrc.2337openalex-snapshot
Variation in protein Cα‐related one‐bond J couplings
inferred← citeshttps://doi.org/10.1002/mrc.3888openalex-snapshot
Review: use of residual dipolar couplings to determine the structure of carbohydrates
inferred← citeshttps://doi.org/10.1002/mrc.3889openalex-snapshot
Influence of solvent and salt concentration on the alignment properties of acrylamide copolymer gels for the measurement of RDC
inferred← citeshttps://doi.org/10.1002/mrc.3895openalex-snapshot
New strategy for RDC‐assisted diastereotopic proton assignment using a combination of J‐scaled BIRD HSQC and J‐scaled BIRD HMQC/HSQC
inferred← citeshttps://doi.org/10.1002/mrc.3902openalex-snapshot
Configuration verification via RDCs on the example of a tetra‐substituted pyrrolidine ring
inferred← citeshttps://doi.org/10.1002/mrc.4400openalex-snapshot
Di(ethylene glycol) methyl ether methacrylate (DEGMEMA)‐derived gels align small organic molecules in methanol
inferred← citeshttps://doi.org/10.1002/mrc.4543openalex-snapshot
Perspectives in the application of residual dipolar couplings in the structure elucidation of weakly aligned small molecules
inferred← citeshttps://doi.org/10.1002/mrc.4921openalex-snapshot
Orientation and conformation of two [6]carbohelicenes in stretched polystyrene and a thermoresponsive polyaspartate
inferred← citeshttps://doi.org/10.1002/mrc.5266openalex-snapshot
A supramolecular and liquid crystalline water‐based alignment medium based on azobenzene‐substituted 1,3,5‐benzenetricarboxamides
inferred← citeshttps://doi.org/10.1002/mrc.5448openalex-snapshot
Hydrogen bond formation may enhance RDC‐based discrimination of enantiomers
inferred← citeshttps://doi.org/10.1002/mrc.5494openalex-snapshot
Reversibly Compressible Cross‐Linked Polystyrene Gels, Compatible With Toluene‐d8 and Pyridine‐d5, for Measurement of Residual Dipolar Couplings and Residual Chemical Shift Anisotropies
inferred← citeshttps://doi.org/10.1002/mrc.5507openalex-snapshot
Cross‐Correlation Between 11 B Quadrupole and 11 B‐ 19 F Dipole–Dipole Coupling in BF 2 Groups
inferred← citeshttps://doi.org/10.1002/mrc.5522openalex-snapshot
Synthesis and Application of a Hydrophobic Polyglutamate Bearing a Triphenylphosphine Group for the Orientation of Pharmaceutically Active Compounds and the Measurement of Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1002/mrc.5523openalex-snapshot
Heterophyllin B: Combining Isotropic and Anisotropic NMR for the Conformational Analysis of a Natural Occurring Cyclic Peptide
inferred← citeshttps://doi.org/10.1002/mrc.70025openalex-snapshot
Chiral Polyacetylene‐PDMS‐Copolymer‐Gels as Enantiodifferentiating Alignment Media
inferred← citeshttps://doi.org/10.1002/mrc.70064openalex-snapshot
Residual Chemical Shift Anisotropies in the Structure Determination of Small Molecules
inferred← citeshttps://doi.org/10.1002/pro.2124openalex-snapshot
Interdomain orientation of cardiac Troponin C characterized by paramagnetic relaxation enhancement NMR reveals a compact state
inferred← citeshttps://doi.org/10.1002/pro.2133openalex-snapshot
Lanthanide binding and IgG affinity construct: Potential applications in solution NMR, MRI, and luminescence microscopy
inferred← citeshttps://doi.org/10.1002/pro.2163openalex-snapshot
Smooth statistical torsion angle potential derived from a large conformational database via adaptive kernel density estimation improves the quality of NMR protein structures
inferred← citeshttps://doi.org/10.1002/pro.219openalex-snapshot
The solution structure and dynamics of the DH‐PH module of PDZRhoGEF in isolation and in complex with nucleotide‐free RhoA
inferred← citeshttps://doi.org/10.1002/pro.2450openalex-snapshot
Solution structure of lysine‐free (K0) ubiquitin
inferred← citeshttps://doi.org/10.1002/pro.2654openalex-snapshot
Structural heterogeneity in microcrystalline ubiquitin studied by solid‐state NMR
inferred← citeshttps://doi.org/10.1002/pro.2770openalex-snapshot
Assessment of the utility of contact‐based restraints in accelerating the prediction of protein structure using molecular dynamics simulations
inferred← citeshttps://doi.org/10.1002/pro.34openalex-snapshot
Residual structure within the disordered C‐terminal segment of p21Waf1/Cip1/Sdi1 and its implications for molecular recognition
inferred← citeshttps://doi.org/10.1002/pro.4922openalex-snapshot
Xplor‐NIH : Better parameters and protocols for NMR protein structure determination
inferred← citeshttps://doi.org/10.1002/pro.584openalex-snapshot
The structure of human ubiquitin in 2‐methyl‐2,4‐pentanediol: A new conformational switch
inferred← citeshttps://doi.org/10.1002/prot.10299openalex-snapshot
Refinement of protein structures in explicit solvent
inferred← citeshttps://doi.org/10.1002/prot.10439openalex-snapshot
Filtering and selection of structural models: Combining docking and NMR
inferred← citeshttps://doi.org/10.1002/prot.10496openalex-snapshot
Relative stability of protein structures determined by X‐ray crystallography or NMR spectroscopy: A molecular dynamics simulation study
inferred← citeshttps://doi.org/10.1002/prot.20320openalex-snapshot
Structure and dynamics of the human pleckstrin DEP domain: Distinct molecular features of a novel DEP domain subfamily
inferred← citeshttps://doi.org/10.1002/prot.20470openalex-snapshot
Long dynamics simulations of proteins using atomistic force fields and a continuum representation of solvent effects: Calculation of structural and dynamic properties
inferred← citeshttps://doi.org/10.1002/prot.20476openalex-snapshot
Various strategies of using residual dipolar couplings in NMR‐driven protein docking: Application to Lys48‐linked di‐ubiquitin and validation against 15 N‐relaxation data
inferred← citeshttps://doi.org/10.1002/prot.20811openalex-snapshot
Evaluating the quality of NMR structures by local density of protons
inferred← citeshttps://doi.org/10.1002/prot.20917openalex-snapshot
Interdomain mobility in di‐ubiquitin revealed by NMR
inferred← citeshttps://doi.org/10.1002/prot.20985openalex-snapshot
Error distribution derived NOE distance restraints
inferred← citeshttps://doi.org/10.1002/prot.21060openalex-snapshot
Modeling protein conformational ensembles: From missing loops to equilibrium fluctuations
inferred← citeshttps://doi.org/10.1002/prot.21063openalex-snapshot
Determination of dihedral Ψ angles in large proteins by combining NHN/CαHα dipole/dipole cross‐correlation and chemical shifts
inferred← citeshttps://doi.org/10.1002/prot.21068openalex-snapshot
The DC‐module of doublecortin: Dynamics, domain boundaries, and functional implications
inferred← citeshttps://doi.org/10.1002/prot.21145openalex-snapshot
Thermal versus mechanical unfolding of ubiquitin
inferred← citeshttps://doi.org/10.1002/prot.21507openalex-snapshot
A large data set comparison of protein structures determined by crystallography and NMR: Statistical test for structural differences and the effect of crystal packing
inferred← citeshttps://doi.org/10.1002/prot.21726openalex-snapshot
Factors affecting the use of 13Cα chemical shifts to determine, refine, and validate protein structures
inferred← citeshttps://doi.org/10.1002/prot.22210openalex-snapshot
Simulated tempering yields insight into the low‐resolution Rosetta scoring functions
inferred← citeshttps://doi.org/10.1002/prot.22568openalex-snapshot
Crystal structures of Lys‐63‐linked tri‐ and di‐ubiquitin reveal a highly extended chain architecture
inferred← citeshttps://doi.org/10.1002/prot.23207openalex-snapshot
Protein loop closure using orientational restraints from NMR data
inferred← citeshttps://doi.org/10.1002/prot.24213openalex-snapshot
Vivaldi: Visualization and validation of biomacromolecular NMR structures from the PDB
inferred← citeshttps://doi.org/10.1002/prot.24280openalex-snapshot
Combined computational design of a zinc‐binding site and a protein–protein interaction: One open zinc coordination site was not a robust hotspot for de novo ubiquitin binding
inferred← citeshttps://doi.org/10.1002/prot.24427openalex-snapshot
BCL::Fold—Protein topology determination from limited NMR restraints
inferred← citeshttps://doi.org/10.1002/prot.25525openalex-snapshot
How accurately do force fields represent protein side chain ensembles?
inferred← citeshttps://doi.org/10.1002/prot.25769openalex-snapshot
Protein structure prediction using sparse NOE and RDC restraints with Rosetta in CASP13
inferred← citeshttps://doi.org/10.1002/prot.70062openalex-snapshot
Predicting Pose Distribution of Protein Domains Connected by Flexible Linkers Is an Unsolved Problem
inferred← citeshttps://doi.org/10.1002/psc.3166openalex-snapshot
Conformational studies of RGDechi peptide by natural‐abundance NMR spectroscopy
inferred← citeshttps://doi.org/10.1002/qua.24166openalex-snapshot
Protein backbone structure determination using RDC: An inverse kinematics approach with fast and exact solutions
inferred← citeshttps://doi.org/10.1006/jmbi.2001.5181openalex-snapshot
Structure and properties of a dimeric N-terminal fragment of human ubiquitin 1 1Edited by R. Huber
inferred← citeshttps://doi.org/10.1006/jmbi.2002.5446openalex-snapshot
Temperature-dependence of protein hydrogen bond properties as studied by high-resolution NMR 1 1Edited by P. E. Wright
inferred← citeshttps://doi.org/10.1006/jmre.1999.1819openalex-snapshot
Accurate Measurement of HN–Hα Residual Dipolar Couplings in Proteins
inferred← citeshttps://doi.org/10.1006/jmre.1999.1985openalex-snapshot
Direct Refinement against Proton–Proton Dipolar Couplings in NMR Structure Determination of Macromolecules
inferred← citeshttps://doi.org/10.1006/jmre.2000.2063openalex-snapshot
Protein Backbone 15N Relaxation Rates as a Tool for the Diagnosis of Structure Quality
inferred← citeshttps://doi.org/10.1006/jmre.2001.2454openalex-snapshot
Specification and Visualization of Anisotropic Interaction Tensors in Polypeptides and Numerical Simulations in Biological Solid-State NMR
inferred← citeshttps://doi.org/10.1006/jmre.2002.2569openalex-snapshot
Assignment Strategy for Proteins with Known Structure
inferred← citeshttps://doi.org/10.1006/jmre.2002.2597openalex-snapshot
Hydrogen Bonds in Human Ubiquitin Reflected in Temperature Coefficients of Amide Protons
inferred← citeshttps://doi.org/10.1007/0-306-47936-2_6openalex-snapshot
NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids
inferred← citeshttps://doi.org/10.1007/0-306-47936-2_7openalex-snapshot
Angular Restraints from Residual Dipolar Couplings for Structure Refinement
inferred← citeshttps://doi.org/10.1007/128_2011_215openalex-snapshot
The Use of Residual Dipolar Coupling in Studying Proteins by NMR
inferred← citeshttps://doi.org/10.1007/978-1-4939-6454-3_14openalex-snapshot
Designing DNA Nanotube Liquid Crystals as a Weak-Alignment Medium for NMR Structure Determination of Membrane Proteins
inferred← citeshttps://doi.org/10.1007/978-1-61779-474-2_20openalex-snapshot
Identifying and Studying Ubiquitin Receptors by NMR
inferred← citeshttps://doi.org/10.1007/978-1-61779-480-3_10openalex-snapshot
Bacterial Production and Solution NMR Studies of a Viral Membrane Ion Channel
inferred← citeshttps://doi.org/10.1007/978-1-61779-480-3_20openalex-snapshot
Electrostatics of Hydrogen Exchange for Analyzing Protein Flexibility
inferred← citeshttps://doi.org/10.1007/978-3-319-06170-2_5openalex-snapshot
Experimental Results
inferred← citeshttps://doi.org/10.1007/978-3-319-28275-6_86-1openalex-snapshot
Residual Dipolar Coupling for Conformational and Dynamic Studies
inferred← citeshttps://doi.org/10.1007/978-3-319-28388-3_86openalex-snapshot
Residual Dipolar Coupling for Conformational and Dynamic Studies
inferred← citeshttps://doi.org/10.1007/978-3-319-95843-9_20openalex-snapshot
13C Chemical Shifts in Proteins: A Rich Source of Encoded Structural Information
inferred← citeshttps://doi.org/10.1007/978-3-540-73433-8_16openalex-snapshot
Protein Structure Prediction Using Residual Dipolar Couplings
inferred← citeshttps://doi.org/10.1007/978-3-540-74029-2_10openalex-snapshot
Protein Folding, Unfolding and Aggregation Studied Using an All-Atom Model with~a~Simplified Interaction Potential
inferred← citeshttps://doi.org/10.1007/978-3-642-12683-3_36openalex-snapshot
A Markov Random Field Framework for Protein Side-Chain Resonance Assignment
inferred← citeshttps://doi.org/10.1007/978-3-642-20036-6_43openalex-snapshot
Protein Loop Closure Using Orientational Restraints from NMR Data
inferred← citeshttps://doi.org/10.1007/978-3-642-28554-7_19openalex-snapshot
13C Chemical Shifts in Proteins: A Rich Source of Encoded Structural Information
inferred← citeshttps://doi.org/10.1007/978-3-642-36077-0_16openalex-snapshot
DNA-Nanotube-Enabled NMR Structure Determination of Membrane Proteins
inferred← citeshttps://doi.org/10.1007/978-3-642-37195-0_25openalex-snapshot
Extracting Structural Information from Residual Chemical Shift Anisotropy: Analytic Solutions for Peptide Plane Orientations and Applications to Determine Protein Structure
inferred← citeshttps://doi.org/10.1007/978-94-017-0221-8_8openalex-snapshot
Observation and Interpretation of Residual Dipolar Couplings in Biomolecules
inferred← citeshttps://doi.org/10.1007/978-94-017-2579-8_9openalex-snapshot
Numerical simulations for experiment design and extraction of structural parameters in biological solid-state NMR spectroscopy
inferred← citeshttps://doi.org/10.1007/bf03167001openalex-snapshot
Temperature-dependent protein backbone dynamics from auto- and cross-correlated NMR relaxation rates
inferred← citeshttps://doi.org/10.1007/s00249-005-0018-6openalex-snapshot
Prediction of charge-induced molecular alignment: residual dipolar couplings at pH 3 and alignment in surfactant liquid crystalline phases
inferred← citeshttps://doi.org/10.1007/s00723-011-0256-yopenalex-snapshot
Quantitative Approach to CIDNP in Proteins with Several Polarizable Residues on the Surface
inferred← citeshttps://doi.org/10.1007/s10858-004-3218-yopenalex-snapshot
Asparagine and glutamine side-chain conformation in solution and crystal: A comparison for hen egg-white lysozyme using residual dipolar ouplings
inferred← citeshttps://doi.org/10.1007/s10858-004-4349-xopenalex-snapshot
Estimates of methyl 13C and 1H CSA values (??) in proteins from cross-correlated spin relaxation
inferred← citeshttps://doi.org/10.1007/s10858-004-5318-0openalex-snapshot
Improved detection of long-range residual dipolar couplings in weakly aligned samples by Lee?Goldburg decoupling of homonuclear dipolar truncation
inferred← citeshttps://doi.org/10.1007/s10858-004-6057-yopenalex-snapshot
Efficient and precise measurement of H??C?, C??C?, C??C? and HN?N residual dipolar couplings from 2D HN?N correlation spectra
inferred← citeshttps://doi.org/10.1007/s10858-004-7563-7openalex-snapshot
A protein backbone ψ and φ angle dependence of 2J N (i) ,Cα1;( i - 1): The new NMR experiment and quantum chemical calculations
showing the first 200 of 908 · page through all 908
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.