On the public citation graph

Dierential Scanning Calorimetry of Proteins and Zimm-Bragg Model in Water

0 signed · 40 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 See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.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/10.1002/1097-4628(20001220)78:13<2262::aid-app40>3.0.co;2-yopenalex-extracted
Determination of activation energy and preexponential factor of thermoset reaction kinetics using differential scanning calorimetry in scanning mode: Influence of baseline shape on different calculation methods
inferredcites →https://doi.org/10.1002/9783527619498openalex-extracted
Protein Folding Handbook
inferredcites →https://doi.org/10.1002/bip.360300313openalex-extracted
Helix‐Coil transition in polypeptides: A microscopical approach
inferredcites →https://doi.org/10.1002/ceat.202100120openalex-extracted
Selection of Formal Baseline Correction Methods in Thermal Analysis
inferredcites →https://doi.org/10.1002/pro.2449openalex-extracted
Contribution of hydrogen bonds to protein stability
inferredcites →https://doi.org/10.1006/abio.1995.9957openalex-extracted
Precise Scanning Calorimeter for Studying Thermal Properties of Biological Macromolecules in Dilute Solution
inferredcites →https://doi.org/10.1006/icar.1993.1010openalex-extracted
Habitable Zones around Main Sequence Stars
inferredcites →https://doi.org/10.1007/bf01913481openalex-extracted
The baseline construction and its influence on the measurement of heat with differential scanning calorimeters
inferredcites →https://doi.org/10.1016/0022-2836(86)90017-3openalex-extracted
Cold denaturation of myoglobin
inferredcites →https://doi.org/10.1016/j.bpc.2006.05.004openalex-extracted
Microcalorimetry of biological macromolecules
inferredcites →https://doi.org/10.1016/j.epsl.2005.06.013openalex-extracted
How Earth's atmosphere evolved to an oxic state: A status report
inferredcites →https://doi.org/10.1016/s0006-3495(96)79397-9openalex-extracted
Thermodynamic effects of mutations on the denaturation of T4 lysozyme
inferredcites →https://doi.org/10.1016/s0006-3495(96)79401-8openalex-extracted
Hydrogen bonding stabilizes globular proteins
inferredcites →https://doi.org/10.1017/s0033583516000044openalex-extracted
Thermal protein unfolding by differential scanning calorimetry and circular dichroism spectroscopy Two-state model versus sequential unfolding
inferredcites →https://doi.org/10.1021/ac60213a020openalex-extracted
The Analysis of a Temperature-Controlled Scanning Calorimeter.
inferredcites →https://doi.org/10.1021/bi00789a002openalex-extracted
Reversible pressure-temperature denaturation of chymotrypsinogen
inferredcites →https://doi.org/10.1021/cr4003177openalex-extracted
Interstellar Water Chemistry: From Laboratory to Observations
inferredcites →https://doi.org/10.1021/ja055996yopenalex-extracted
Direct Measurement of Barrier Heights in Protein Folding
inferredcites →https://doi.org/10.1021/ja110884mopenalex-extracted
Quantitative Prediction of Protein Folding Behaviors from a Simple Statistical Model
inferredcites →https://doi.org/10.1021/ja801401aopenalex-extracted
Expanding the Realm of Ultrafast Protein Folding: gpW, a Midsize Natural Single-Domain with α+β Topology that Folds Downhill
inferredcites →https://doi.org/10.1021/jp961825ropenalex-extracted
Free Energy of Amide Hydrogen Bond Formation in Vacuum, in Water, and in Liquid Alkane Solution
inferredcites →https://doi.org/10.1038/s41550-022-01700-4openalex-extracted
Liquid water on planets with a primordial atmosphere can be long-lasting
inferredcites →https://doi.org/10.1038/s41598-017-16360-yopenalex-extracted
Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating
inferredcites →https://doi.org/10.1038/s42004-021-00499-xopenalex-extracted
Implicit water model within the Zimm-Bragg approach to analyze experimental data for heat and cold denaturation of proteins
inferredcites →https://doi.org/10.1063/1.1696442openalex-extracted
On the Temperature Dependence of Cooperative Relaxation Properties in Glass-Forming Liquids
inferredcites →https://doi.org/10.1063/1.1730390openalex-extracted
Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains
inferredcites →https://doi.org/10.1073/pnas.0405829101openalex-extracted
Exploring protein-folding ensembles: A variable-barrier model for the analysis of equilibrium unfolding experiments
inferredcites →https://doi.org/10.1073/pnas.1612480114openalex-extracted
Origin of hydrophobicity and enhanced water hydrogen bond strength near purely hydrophobic solutes
inferredcites →https://doi.org/10.1073/pnas.1703781114openalex-extracted
Water is an active matrix of life for cell and molecular biology
inferredcites →https://doi.org/10.1073/pnas.200343197openalex-extracted
Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities
inferredcites →https://doi.org/10.1073/pnas.2133366100openalex-extracted
Energetics of hydrogen bonds in peptides
inferredcites →https://doi.org/10.1074/jbc.m010770200openalex-extracted
Strength of the CαH··O Hydrogen Bond of Amino Acid Residues
inferredcites →https://doi.org/10.1089/15311070260192246openalex-extracted
Remote Sensing of Planetary Properties and Biosignatures on Extrasolar Terrestrial Planets
inferredcites →https://doi.org/10.1089/15311070260192264openalex-extracted
Reassessing the Possibility of Life on Venus: Proposal for an Astrobiology Mission
inferredcites →https://doi.org/10.1093/protein/13.7.501openalex-extracted
Thermal unfolding and conformational stability of the recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima
inferredcites →https://doi.org/10.1103/physreve.81.021921openalex-extracted
Microscopic formulation of the Zimm-Bragg model for the helix-coil transition
inferredcites →https://doi.org/10.1103/physreve.89.022723openalex-extracted
Unified description of solvent effects in the helix-coil transition
inferredcites →https://doi.org/10.1351/pac200779081445openalex-extracted
Thermodynamic problems in structural molecular biology
inferredcites →https://doi.org/10.1385/0896033015openalex-extracted
Protein Stability and Folding
inferredcites →https://doi.org/10.3390/polym13121985openalex-extracted
System Size Dependence in the Zimm–Bragg Model: Partition Function Limits, Transition Temperature and Interval
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.