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Rational Modification of Protein Stability by the Mutation of Charged Surface Residues
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Conformational analysis of peptide fragments derived from the peripheral subunit-binding domain from the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: Evidence for nonrandom structure in the unfolded state
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CHARMM : A program for macromolecular energy, minimization, and dynamics calculations
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The High-resolution Structure of the Peripheral Subunit-binding Domain of Dihydrolipoamide Acetyltransferase from the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilus
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Cooperative folding of a protein mini domain: the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex 1 1Edited by P. E. Wright
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Electrostatic contributions to the stability of hyperthermophilic proteins
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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
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Analytical ultracentrifugation in biochemistry and polymer science
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Experiments in Physical Chemistry
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Strength and co-operativity of contributions of surface salt bridges to protein stability
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Electrostatics in biomolecular structure and dynamics
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Experiments in physical chemistry
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Accurate Calculation of Hydration Free Energies Using Macroscopic Solvent Models
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Parameter Dependence in Continuum Electrostatic Calculations: A Study Using Protein Salt Bridges
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NMR of Proteins and Nucleic Acids
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Electrostatic Interactions in Macromolecules: Theory and Applications
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inferred← citeshttps://doi.org/10.1073/pnas.0808220106openalex-snapshot
Rational stabilization of enzymes by computational redesign of surface charge–charge interactions
inferred← citeshttps://doi.org/10.1073/pnas.0837456100openalex-snapshot
Hydrogen-exchange stability analysis of Bergerac -Src homology 3 variants allows the characterization of a folding intermediate in equilibrium
inferred← citeshttps://doi.org/10.1073/pnas.1222245110openalex-snapshot
Rational modification of protein stability by targeting surface sites leads to complicated results
inferred← citeshttps://doi.org/10.1073/pnas.1406845111openalex-snapshot
Residue level quantification of protein stability in living cells
inferred← citeshttps://doi.org/10.1073/pnas.1417415112openalex-snapshot
Quinary structure modulates protein stability in cells
inferred← citeshttps://doi.org/10.1073/pnas.1818744116openalex-snapshot
Networks of electrostatic and hydrophobic interactions modulate the complex folding free energy surface of a designed βα protein
inferred← citeshttps://doi.org/10.1074/jbc.m109.033894openalex-snapshot
Electrostatic Interactions of Hsp-organizing Protein Tetratricopeptide Domains with Hsp70 and Hsp90
inferred← citeshttps://doi.org/10.1074/jbc.m504216200openalex-snapshot
Identifying and Engineering Ion Pairs in Adenylate Kinases
inferred← citeshttps://doi.org/10.1080/07388551.2021.2004084openalex-snapshot
Strategies for tailoring pH performances of glycoside hydrolases
inferred← citeshttps://doi.org/10.1080/07391102.2004.10506967openalex-snapshot
Thermophilicity of Wild Type and Mutant Cold Shock Proteins by Molecular Dynamics Simulation
inferred← citeshttps://doi.org/10.1080/1521654031000123330openalex-snapshot
Heterotachy and Functional Shift in Protein Evolution
inferred← citeshttps://doi.org/10.1080/20014091074174openalex-snapshot
Thermophilic Adaptation of Proteins
inferred← citeshttps://doi.org/10.1088/1478-3975/14/1/013002openalex-snapshot
Linking computation and experiments to study the role of charge–charge interactions in protein folding and stability
inferred← citeshttps://doi.org/10.1093/nar/gkr171openalex-snapshot
Paired mutations abolish and restore the balanced annealing and melting activities of ORF1p that are required for LINE-1 retrotransposition
inferred← citeshttps://doi.org/10.1093/protein/14.12.961openalex-snapshot
High thermal stability of 3-isopropylmalate dehydrogenase from Thermus thermophilus resulting from low ΔΔCp of unfolding
inferred← citeshttps://doi.org/10.1093/protein/gzg103openalex-snapshot
Effect of mutations involving charged residues on the stability of staphylococcal nuclease: a continuum electrostatics study
inferred← citeshttps://doi.org/10.1093/protein/gzg131openalex-snapshot
Optimized electrostatic surfaces parallel increased thermostability: a structural bioinformatic analysis
inferred← citeshttps://doi.org/10.1093/protein/gzi051openalex-snapshot
How to improve nature: study of the electrostatic properties of the surface of α-lactalbumin
inferred← citeshttps://doi.org/10.1093/protein/gzr004openalex-snapshot
Modulating the pH-activity profile of cellulase A from Cellulomonas fimi by replacement of surface residues
inferred← citeshttps://doi.org/10.1093/protein/gzt007openalex-snapshot
Thermal stability engineering of Glomerella cingulata cutinase
inferred← citeshttps://doi.org/10.1093/protein/gzw014openalex-snapshot
Electrostatic effects on the folding stability of FKBP12
inferred← citeshttps://doi.org/10.1110/ps.0209302openalex-snapshot
Functional aspects of co‐variant surface charges in an antibody fragment
inferred← citeshttps://doi.org/10.1110/ps.0227903openalex-snapshot
Electrostatic interactions in the reconstitution of an SH2 domain from constituent peptide fragments
inferred← citeshttps://doi.org/10.1110/ps.0302303openalex-snapshot
Solution structure and thermal stability of ribosomal protein L30e from hyperthermophilic archaeon Thermococcus celer
inferred← citeshttps://doi.org/10.1110/ps.03486104openalex-snapshot
Energy functions for protein design I: Efficient and accurate continuum electrostatics and solvation
inferred← citeshttps://doi.org/10.1110/ps.051401905openalex-snapshot
Charge–charge interactions in the denatured state influence the folding kinetics of ribonuclease Sa
inferred← citeshttps://doi.org/10.1110/ps.051405005openalex-snapshot
Glucosylation of β‐lactoglobulin lowers the heat capacity change of unfolding; a unique way to affect protein thermodynamics
inferred← citeshttps://doi.org/10.1110/ps.073091607openalex-snapshot
Computational design of the Fyn SH3 domain with increased stability through optimization of surface charge–charge interactions
inferred← citeshttps://doi.org/10.1110/ps.17601openalex-snapshot
Understanding thermostability in cytochrome P450 by combinatorial mutagenesis
inferred← citeshttps://doi.org/10.1110/ps.2980102openalex-snapshot
Salt‐induced stabilization of apoflavodoxin at neutral pH is mediated through cation‐specific effects
inferred← citeshttps://doi.org/10.1110/ps.29902openalex-snapshot
Removal of surface charge-charge interactions from ubiquitin leaves the protein folded and very stable
inferred← citeshttps://doi.org/10.1110/ps.4700102openalex-snapshot
Distance dependence and salt sensitivity of pairwise, coulombic interactions in a protein
inferred← citeshttps://doi.org/10.1110/ps.9.10.2026openalex-snapshot
Dimer formation by a “monomeric” protein
inferred← citeshttps://doi.org/10.1110/ps.9.7.1395openalex-snapshot
Charge–charge interactions influence the denatured state ensemble and contribute to protein stability
inferred← citeshttps://doi.org/10.1111/j.1742-4658.2009.06910.xopenalex-snapshot
Engineering thermal stability of l‐ asparaginase by in vitro directed evolution
inferred← citeshttps://doi.org/10.1128/jb.185.14.4285-4289.2003openalex-snapshot
An Integrated Structural and Computational Study of the Thermostability of Two Thioredoxin Mutants fromAlicyclobacillus acidocaldarius
inferred← citeshttps://doi.org/10.1134/s0003683822060151openalex-snapshot
The Thermostability of Nucleoside Phosphorylases from Prokaryotes. I. The Role of the Primary Structure of the N-terminal fragment of the Protein in the Thermostability of Uridine Phosphorylases
inferred← citeshttps://doi.org/10.1186/1471-2091-5-9openalex-snapshot
Mutation of exposed hydrophobic amino acids to arginine to increase protein stability
inferred← citeshttps://doi.org/10.1186/1471-2105-8-s1-s15openalex-snapshot
Environment specific substitution tables for thermophilic proteins
inferred← citeshttps://doi.org/10.1186/1472-6807-7-18openalex-snapshot
Mechanisms for stabilisation and the maintenance of solubility in proteins from thermophiles
inferred← citeshttps://doi.org/10.1186/s13568-017-0405-2openalex-snapshot
Thermostabilization of the uronate dehydrogenase from Agrobacterium tumefaciens by semi-rational design
inferred← citeshttps://doi.org/10.1246/cl.190875openalex-snapshot
Engineered Protein-tag for Rapid Live-cell Fluorogenic Visualization of Proteins by Anionic Probes
inferred← citeshttps://doi.org/10.1371/journal.pbio.1001027openalex-snapshot
A Rigidifying Salt-Bridge Favors the Activity of Thermophilic Enzyme at High Temperatures at the Expense of Low-Temperature Activity
inferred← citeshttps://doi.org/10.1371/journal.pone.0190816openalex-snapshot
Investigation of the proton relay system operative in human cystosolic aminopeptidase P
inferred← citeshttps://doi.org/10.1529/biophysj.104.049189openalex-snapshot
Electrostatic Contributions to the Kinetics and Thermodynamics of Protein Assembly
inferred← citeshttps://doi.org/10.17760/d20003102openalex-snapshot
Optical tweezers reveal how proteins alter replication
inferred← citeshttps://doi.org/10.2174/092986610789909502openalex-snapshot
Identification and Characterization of Molten Globule-Like State of Hen Egg-White Lysozyme in Presence of Salts Under Alkaline Conditions
inferred← citeshttps://doi.org/10.2174/0929867325666181017160857openalex-snapshot
From Levinthal’s Paradox to the Effects of Cell Environmental Perturbation on Protein Folding
inferred← citeshttps://doi.org/10.2174/157016407781387375openalex-snapshot
Conformational States and Protein Stability from a Proteomic Perspective
inferred← citeshttps://doi.org/10.31390/gradschool_dissertations.3815openalex-snapshot
Residue coevolution: modeling and interpretation
inferred← citeshttps://doi.org/10.57709/1059259openalex-snapshot
Using Protein Design to Understand the Role of Electrostatic Interactions on Calcium Binding Affinity and Molecular Recognition
inferred← citeshttps://doi.org/10.5772/53330openalex-snapshot
Site-Directed Mutagenesis as Applied to Biocatalysts
inferred← citeshttps://doi.org/10.5821/dissertation-2117-106489openalex-snapshot
Quantum chemistry and conformational sampling meet together : a powerful approach to study and design metalloprotein reactivity
inferred← citeshttps://doi.org/10.5897/ijbmbr12.012openalex-snapshot
Enhancing thermostability of the biocatalysts beyond their natural function via protein engineering
inferred← citeshttps://doi.org/10.7916/d8fb50xhopenalex-snapshot
Engineering heterogeneous biocatalysis
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