The effect of the polyproline II (PPII) conformation on the denatured state entropy.
about
SH3 domains of Grb2 adaptor bind to PXpsiPXR motifs within the Sos1 nucleotide exchange factor in a discriminate mannerThe high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3High-resolution crystal structure of spectrin SH3 domain fused with a proline-rich peptideMolecular determinants of TRIF proteolysis mediated by the hepatitis C virus NS3/4A proteaseBinding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAblIdentification of polyproline II regions derived from the proline-rich nuclear receptor coactivators PNRC and PNRC2: new insights for ERα coactivator interactions.Interfacial water molecules in SH3 interactions: Getting the full picture on polyproline recognition by protein-protein interaction domains.Characterizing 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.A binding event converted into a folding event.Elongated polyproline motifs facilitate enamel evolution through matrix subunit compaction.What can solid state NMR contribute to our understanding of protein folding?Polyproline II helix conformation in a proline-rich environment: a theoretical study.Coupled folding and binding of the disordered protein PUMA does not require particular residual structure.Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Impacts of terminal (4R)-fluoroproline and (4S)-fluoroproline residues on polyproline conformation.Protein-solvent interactionsAn improved experimental system for determining small folding entropy changes resulting from proline to alanine substitutionsReducing the dimensionality of the protein-folding search problem.Reassessing random-coil statistics in unfolded proteins.Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites.Recent advances on polyproline II.Concerted millisecond timescale dynamics in the intrinsically disordered carboxyl terminus of γ-tubulin induced by mutation of a conserved tyrosine residue.
P2860
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P2860
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
description
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2003 թվականի մարտին հրատարակված գիտական հոդված
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2003年の論文
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2003年論文
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2003年論文
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name
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
@ast
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
@en
type
label
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
@ast
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
@en
prefLabel
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
@ast
The effect of the polyproline II (PPII) conformation on the denatured state entropy.
@en
P2860
P356
P1433
P1476
The effect of the polyproline II (PPII) conformation on the denatured state entropy
@en
P2093
Vincent J Hilser
P2860
P304
P356
10.1110/PS.0237803
P577
2003-03-01T00:00:00Z