On the Structure of Native, Denatured, and Coagulated Proteins
about
Native aggregation as a cause of origin of temporary cellular structures needed for all forms of cellular activity, signaling and transformationsEnergetics of protein hydrogen bondsNucleation, rapid folding, and globular intrachain regions in proteinsCoherent Behavior and the Bound State of Water and K(+) Imply Another Model of Bioenergetics: Negative Entropy Instead of High-energy Bondsn-->pi* interactions in proteinsPolymer principles and protein foldingA backbone-based theory of protein foldingReminiscences from a life in protein physical chemistryContribution of hydrogen bonds to protein stabilityEarly Theories of Protein StructureNatively unfolded proteins: a point where biology waits for physicsSequence complexity of disordered proteinConformational stability of CopC and roles of residues Tyr79 and Trp83.Metastability of the folded states of globular proteins.Energetics of hydrogen bonds in peptides.Protein structure, stability and solubility in water and other solvents.An effective evolutionary algorithm for protein folding on 3D FCC HP model by lattice rotation and generalized move sets.Strength of a bifurcated H bond.Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.Structures, basins, and energies: a deconstruction of the Protein Coil Library.Quinary structure modulates protein stability in cells.Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.On the satisfaction of backbone-carbonyl lone pairs of electrons in protein structures.Proteins of the Nervous System: Considered in the Light of the Prevailing Hypotheses on Protein Structure.Structural gymnastics of multifunctional metamorphic proteins.An effective hybrid of hill climbing and genetic algorithm for 2D triangular protein structure prediction.Principles of protein folding--a perspective from simple exact models.The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.Unfoldomics of human diseases: linking protein intrinsic disorder with diseasesMercaptan-induced coagulation of proteinsDifferences in the processes of beta-lactoglobulin cold and heat denaturationsA brief history of the journal of general physiology.How protein chemists learned about the hydrophobic factor.The structural basis of urea-induced protein unfolding in β-cateninDevelopment of an ELISA for evaluation of swab recovery efficiencies of bovine serum albumin.A molecular mechanism for osmolyte-induced protein stabilityIntrinsic disorder and functional proteomics.Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A Using H/D Fractionation FactorsOn the thermodynamics of cell injury. Some insights into the molecular mechanisms.Protein folding--what's the question?
P2860
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P2860
On the Structure of Native, Denatured, and Coagulated Proteins
description
1936 nî lūn-bûn
@nan
1936 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1936 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1936年の論文
@ja
1936年論文
@yue
1936年論文
@zh-hant
1936年論文
@zh-hk
1936年論文
@zh-mo
1936年論文
@zh-tw
1936年论文
@wuu
name
On the Structure of Native, Denatured, and Coagulated Proteins
@ast
On the Structure of Native, Denatured, and Coagulated Proteins
@en
type
label
On the Structure of Native, Denatured, and Coagulated Proteins
@ast
On the Structure of Native, Denatured, and Coagulated Proteins
@en
prefLabel
On the Structure of Native, Denatured, and Coagulated Proteins
@ast
On the Structure of Native, Denatured, and Coagulated Proteins
@en
P2860
P356
P1476
On the Structure of Native, Denatured, and Coagulated Proteins
@en
P2093
P2860
P304
P356
10.1073/PNAS.22.7.439
P407
P577
1936-07-01T00:00:00Z