Temperature dependence of the hydrophobic interaction in protein folding
about
Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNAInteratomic potentials and solvation parameters from protein engineering data for buried residuesStructural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylationStructural and energetic basis of allosteryA bottom-up approach to understanding protein layer formation at solid-liquid interfaces.Rigidification of a Flexible Protease Inhibitor Variant upon Binding to TrypsinThermodynamic description of the effect of the mutation Y49F on human glutathione transferase P1-1 in binding with glutathione and the inhibitor S-hexylglutathioneOrigin of Heat Capacity Changes in a “Nonclassical” Hydrophobic InteractionStatistical Coupling Analysis of Aspartic Proteinases Based on Crystal Structures of the Trichoderma reesei Enzyme and Its Complex with Pepstatin AStructural Insight into the Kinetics and Cp of Interactions between TEM-1 -Lactamase and -Lactamase Inhibitory Protein (BLIP)The Contribution of Entropy, Enthalpy, and Hydrophobic Desolvation to Cooperativity in Repeat-Protein FoldingStabilizing Salt-Bridge Enhances Protein Thermostability by Reducing the Heat Capacity Change of UnfoldingCavities determine the pressure unfolding of proteinsCrystal structures and inhibitor binding properties of plant class V chitinases: the cycad enzyme exhibits unique structural and functional featuresBound water molecules and conformational stabilization help mediate an antigen-antibody associationInterplay of structure and disorder in cochaperonin mobile loopsThe Co-crystal structure of staphylococcal enterotoxin type A with Zn2+ at 2.7 A resolution. Implications for major histocompatibility complex class II bindingSec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Influence of Glu-376 --> Gln mutation on enthalpy and heat capacity changes for the binding of slightly altered ligands to medium chain acyl-CoA dehydrogenaseCharacterizing the role of ensemble modulation in mutation-induced changes in binding affinityExploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain.Predicting binding energetics from structure: looking beyond DeltaG degrees.Thermodynamic propensities of amino acids in the native state ensemble: implications for fold recognition.Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.Temperature, stability, and the hydrophobic interactionKinetic and thermodynamic study of the bacteriorhodopsin photocycle over a wide pH range.Energetics of hydrogen bonding in proteins: a model compound studyDo hydration dynamics follow the structural perturbation during thermal denaturation of a protein: a terahertz absorption study.A linkage analysis toolkit for studying allosteric networks in ion channels.Cross-strand interactions of fluorinated amino acids in β-hairpin constructs.High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.Interaction of a designed interleukin-10 epitope mimic with an antibody studied by isothermal titration microcalorimetry.Signatures of protein thermal denaturation and local hydrophobicity in domain specific hydration behavior: a comparative molecular dynamics study.Analysis of the "thermodynamic information content" of a Homo sapiens structural database reveals hierarchical thermodynamic organization.Thermodynamic analysis of acetylation-dependent Pb1 bromodomain-histone H3 interactionsRelation between the convergence temperatures Th* and Ts* in protein unfolding.The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins.Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.Two distinct motifs within the p53 transactivation domain bind to the Taz2 domain of p300 and are differentially affected by phosphorylationThermodynamic and structural analysis of microtubule assembly: the role of GTP hydrolysis.
P2860
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P2860
Temperature dependence of the hydrophobic interaction in protein folding
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh
1986年學術文章
@zh-hant
name
Temperature dependence of the hydrophobic interaction in protein folding
@en
Temperature dependence of the hydrophobic interaction in protein folding.
@nl
type
label
Temperature dependence of the hydrophobic interaction in protein folding
@en
Temperature dependence of the hydrophobic interaction in protein folding.
@nl
prefLabel
Temperature dependence of the hydrophobic interaction in protein folding
@en
Temperature dependence of the hydrophobic interaction in protein folding.
@nl
P2860
P356
P1476
Temperature dependence of the hydrophobic interaction in protein folding
@en
P2093
R L Baldwin
P2860
P304
P356
10.1073/PNAS.83.21.8069
P407
P577
1986-11-01T00:00:00Z