In search of the energetic role of peptide hydrogen bonds.
about
Misfolding and amyloid aggregation of apomyoglobinDirecting macromolecular conformation through halogen bondsThe Trp-cage: optimizing the stability of a globular miniproteinSub-nanoscale surface ruggedness provides a water-tight seal for exposed regions in soluble protein structure.The polyproline II conformation in short alanine peptides is noncooperativeOrigin of the neighboring residue effect on peptide backbone conformation.Building native protein conformation from highly approximate backbone torsion angles.Enthalpy of helix-coil transition: missing link in rationalizing the thermodynamics of helix-forming propensities of the amino acid residuesSpecific collapse followed by slow hydrogen-bond formation of beta-sheet in the folding of single-chain monellinEnd-to-end distance distributions and intrachain diffusion constants in unfolded polypeptide chains indicate intramolecular hydrogen bond formationLysine and arginine residues do not increase the helicity of alanine-rich peptide helices.Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness.Estimation of Hydrogen-Exchange Protection Factors from MD Simulation Based on Amide Hydrogen Bonding Analysis.Do all backbone polar groups in proteins form hydrogen bonds?Functional analysis of an aspartate-based epoxidation catalyst with amide-to-alkene peptidomimetic catalyst analogues.Simple Biophysical Model Predicts Faster Accumulation of Hybrid Incompatibilities in Small Populations Under Stabilizing SelectionHydrogen-bonding and packing features of membrane proteins: functional implicationsStructural insights for designed alanine-rich helices: comparing NMR helicity measures and conformational ensembles from molecular dynamics simulationProbing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.n→π* Interactions Are Competitive with Hydrogen Bonds.Membrane protein folding: how important are hydrogen bonds?STITCHER: Dynamic assembly of likely amyloid and prion β-structures from secondary structure predictions.Counting peptide-water hydrogen bonds in unfolded proteins.Translational-entropy gain of solvent upon protein folding.Genetic selection reveals the role of a buried, conserved polar residue.Physical-chemical determinants of turn conformations in globular proteins.Peptide translocators with engineered dehydration-prone hydrogen bonds.Thermodynamics of apoplastocyanin folding: comparison between experimental and theoretical results.Interfacial Physics for Water in Biology
P2860
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P2860
In search of the energetic role of peptide hydrogen bonds.
description
2003 nî lūn-bûn
@nan
2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
In search of the energetic role of peptide hydrogen bonds.
@ast
In search of the energetic role of peptide hydrogen bonds.
@en
type
label
In search of the energetic role of peptide hydrogen bonds.
@ast
In search of the energetic role of peptide hydrogen bonds.
@en
prefLabel
In search of the energetic role of peptide hydrogen bonds.
@ast
In search of the energetic role of peptide hydrogen bonds.
@en
P2860
P356
P1476
In search of the energetic role of peptide hydrogen bonds.
@en
P2093
Robert L Baldwin
P2860
P304
17581-17588
P356
10.1074/JBC.X200009200
P407
P577
2003-02-11T00:00:00Z