Polyproline II helix conformation in a proline-rich environment: a theoretical study.
about
Krüppel-like factor 11 regulates the expression of metabolic genes via an evolutionarily conserved protein interaction domain functionally disrupted in maturity onset diabetes of the young.Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain.Improved atomistic Monte Carlo simulations demonstrate that poly-L-proline adopts heterogeneous ensembles of conformations of semi-rigid segments interrupted by kinks.Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4.Origin of the neighboring residue effect on peptide backbone conformation.Further evidence for the absence of polyproline II stretch in the XAO peptide.Relevant elements of a maize gamma-zein domain involved in protein body biogenesis.Disorder and order in unfolded and disordered peptides and proteins: a view derived from tripeptide conformational analysis. I. Tripeptides with long and predominantly hydrophobic side chains.A statistical analysis of the PPII propensity of amino acid guests in proline-rich peptides.The alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations.Preferred peptide backbone conformations in the unfolded state revealed by the structure analysis of alanine-based (AXA) tripeptides in aqueous solution.Conformations and free energy landscapes of polyproline peptides.Reassessing random-coil statistics in unfolded proteins.Conformational propensities and residual structures in unfolded peptides and proteins.Evolutionary conservation of the polyproline II conformation surrounding intrinsically disordered phosphorylation sites.UV resonance Raman investigation of the conformations and lowest energy allowed electronic excited states of tri- and tetraalanine: charge transfer transitions.UV resonance raman investigation of electronic transitions in alpha-helical and polyproline II-like conformationsA classical molecular dynamics investigation of the free energy and structure of short polyproline conformers.Isolation and identification of cryptic bioactive regions in bovine achilles tendon collagen.The polypeptide biophysics of proline/alanine-rich sequences (PAS): Recombinant biopolymers with PEG-like properties.Silaproline, a Silicon-Containing Proline Surrogate
P2860
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P2860
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
description
2004 nî lūn-bûn
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2004 թուականի Փետրուարին հրատարակուած գիտական յօդուած
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2004 թվականի փետրվարին հրատարակված գիտական հոդված
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年论文
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name
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@ast
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@en
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@nl
type
label
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@ast
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@en
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@nl
prefLabel
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@ast
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@en
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@nl
P2093
P2860
P1433
P1476
Polyproline II helix conformation in a proline-rich environment: a theoretical study.
@en
P2093
Avijit Ghosh
Daniel R Ripoll
Héctor A Baldoni
Jorge A Vila
P2860
P304
P356
10.1016/S0006-3495(04)74151-X
P407
P577
2004-02-01T00:00:00Z