Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.
about
A backbone-based theory of protein foldingLocal order in the unfolded state: conformational biases and nearest neighbor interactionsAssignment of PolyProline II conformation and analysis of sequence--structure relationshipThe proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro.Identification of polyproline II regions derived from the proline-rich nuclear receptor coactivators PNRC and PNRC2: new insights for ERα coactivator interactions.Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.Effects of solvents on the intrinsic propensity of peptide backbone conformations.Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.Further evidence for the absence of polyproline II stretch in the XAO peptide.Are current molecular dynamics force fields too helical?Acidic-basic properties of three alanine-based peptides containing acidic and basic side chains: comparison between theory and experiment.Polar or apolar--the role of polarity for urea-induced protein denaturationEvaluating the performance of the ff99SB force field based on NMR scalar coupling data.Amino acids with hydrogen-bonding side chains have an intrinsic tendency to sample various turn conformations in aqueous solution.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 study of the influence of charged residues on β-hairpin formation by nuclear magnetic resonance and molecular dynamicsA statistical analysis of the PPII propensity of amino acid guests in proline-rich peptides.A maximum entropy approach to the study of residue-specific backbone angle distributions in α-synuclein, an intrinsically disordered protein.Synthesis and Self-Assembly of a Mikto-Arm Star Dual Drug Amphiphile Containing both Paclitaxel and Camptothecin.Studies on titin PEVK peptides and their interaction.Secondary structure provides a template for the folding of nearby polypeptides.The alanine-rich XAO peptide adopts a heterogeneous population, including turn-like and polyproline II conformations.Insights into Unfolded Proteins from the Intrinsic ϕ/ψ Propensities of the AAXAA Host-Guest Series.Like-charged residues at the ends of oligoalanine sequences might induce a chain reversal.Conformational sampling of peptides in cellular environments.Influence of the Length of the Alanine Spacer on the Acidic-Basic Properties of the Ac-Lys-(Ala)(n)-Lys-NH(2) Peptides (n = 0, 1, 2, …, 5).Assessing the solvent-dependent surface area of unfolded proteins using an ensemble modelPhosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein.J-coupling constants for a trialanine peptide as a function of dihedral angles calculated by density functional theory over the full Ramachandran spaceStructural landscape of the proline-rich domain of Sos1 nucleotide exchange factorSecondary structure bias in generalized Born solvent models: comparison of conformational ensembles and free energy of solvent polarization from explicit and implicit solvationAlpha-Helix folding in the presence of structural constraints.Characterizing aqueous solution conformations of a peptide backbone using Raman optical activity computations.The relationship between water bridges and the polyproline II conformation: a large-scale analysis of molecular dynamics simulations and crystal structures.Conformations and free energy landscapes of polyproline peptides.Structure of Penta-Alanine Investigated by Two-Dimensional Infrared Spectroscopy and Molecular Dynamics SimulationMolecular simulations of protein disorder.Conformational propensities and residual structures in unfolded peptides and proteins.Intrinsically disordered proteins: from sequence and conformational properties toward drug discovery.Multiscale ensemble modeling of intrinsically disordered proteins: p53 N-terminal domain.
P2860
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P2860
Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins.
description
2006 nî lūn-bûn
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2006 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2006 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2006年の論文
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2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Polyproline II conformation is ...... nfolded peptides and proteins.
@ast
Polyproline II conformation is ...... nfolded peptides and proteins.
@en
Polyproline II conformation is ...... nfolded peptides and proteins.
@nl
type
label
Polyproline II conformation is ...... nfolded peptides and proteins.
@ast
Polyproline II conformation is ...... nfolded peptides and proteins.
@en
Polyproline II conformation is ...... nfolded peptides and proteins.
@nl
prefLabel
Polyproline II conformation is ...... nfolded peptides and proteins.
@ast
Polyproline II conformation is ...... nfolded peptides and proteins.
@en
Polyproline II conformation is ...... nfolded peptides and proteins.
@nl
P2093
P2860
P50
P356
P1476
Polyproline II conformation is ...... unfolded peptides and proteins
@en
P2093
Harold A Scheraga
Joanna Makowska
Katarzyna Bagińska
P2860
P304
P356
10.1073/PNAS.0510549103
P407
P577
2006-01-30T00:00:00Z