Solvation energetics and conformational change in EF-hand proteins
about
Conformational and thermodynamic properties of peptide binding to the human S100P proteinThe EF-hand domain: a globally cooperative structural unitA high-resolution structure of the EF-hand domain of human polycystin-2Origins of the difference in Ca2+ requirement for activation of mu- and m-calpainPhenylalanine fluorescence studies of calcium binding to N-domain fragments of Paramecium calmodulin mutants show increased calcium affinity correlates with increased disorderCalcium binding to calmodulin mutants monitored by domain-specific intrinsic phenylalanine and tyrosine fluorescence.Modulation of calmodulin lobes by different targets: an allosteric model with hemiconcerted conformational transitionsRelating form and function of EF-hand calcium binding proteins.The change of protein intradomain mobility on ligand binding: is it a commonly observed phenomenon?Effects of PKA phosphorylation of cardiac troponin I and strong crossbridge on conformational transitions of the N-domain of cardiac troponin C in regulated thin filaments.Thermodynamic basis for the optimization of binding-induced biomolecular switches and structure-switching biosensors.Use of sequence duplication to engineer a ligand-triggered, long-distance molecular switch in T4 lysozyme.New potential uses for cardiac troponins.Protein-protein interactions: principles, techniques, and their potential role in new drug development.Functional and structural analysis of the conserved EFhd2 protein.A molecular dynamics study of Ca(2+)-calmodulin: evidence of interdomain coupling and structural collapse on the nanosecond timescale.Pathogenesis associated with a restrictive cardiomyopathy mutant in cardiac troponin T is due to reduced protein stability and greatly increased myofilament Ca2+ sensitivity.Rational design of a conformation-switchable Ca2+- and Tb3+-binding protein without the use of multiple coupled metal-binding sites.Identification of regions responsible for the open conformation of S100A10 using chimaeric S100A11-S100A10 proteins.Energy functions for protein design I: efficient and accurate continuum electrostatics and solvation.DC3, the smallest subunit of the Chlamydomonas flagellar outer dynein arm-docking complex, is a redox-sensitive calcium-binding protein.Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C.Residue-residue interactions regulating the Ca2+-induced EF-hand conformation changes in calmodulin.
P2860
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P2860
Solvation energetics and conformational change in EF-hand proteins
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Solvation energetics and conformational change in EF-hand proteins
@ast
Solvation energetics and conformational change in EF-hand proteins
@en
Solvation energetics and conformational change in EF-hand proteins
@nl
type
label
Solvation energetics and conformational change in EF-hand proteins
@ast
Solvation energetics and conformational change in EF-hand proteins
@en
Solvation energetics and conformational change in EF-hand proteins
@nl
prefLabel
Solvation energetics and conformational change in EF-hand proteins
@ast
Solvation energetics and conformational change in EF-hand proteins
@en
Solvation energetics and conformational change in EF-hand proteins
@nl
P2860
P356
P1433
P1476
Solvation energetics and conformational change in EF-hand proteins
@en
P2093
J R Desjarlais
P2860
P304
P356
10.1110/PS.33601
P407
P577
2001-02-01T00:00:00Z