Polyproline II structure in a sequence of seven alanine residues. - Wikidata - wikimedia - TriplyDB

Polyproline II structure in a sequence of seven alanine residues.

Polyproline II structure in a sequence of seven alanine residues.

http://www.wikidata.org/entity/Q34034318

about

Pauling and Corey's alpha-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease A backbone-based theory of protein folding Local order in the unfolded state: conformational biases and nearest neighbor interactions UV resonance Raman investigations of peptide and protein structure and dynamics Optimization of Protein Backbone Dihedral Angles by Means of Hamiltonian Reweighting Assignment of PolyProline II conformation and analysis of sequence--structure relationship Comparison of multiple Amber force fields and development of improved protein backbone parameters The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure Formation of partially ordered oligomers of amyloidogenic hexapeptide (NFGAIL) in aqueous solution observed in molecular dynamics simulations.The role of Phe in the formation of well-ordered oligomers of amyloidogenic hexapeptide (NFGAIL) observed in molecular dynamics simulations with explicit solvent.Calculation of the free energy and cooperativity of protein folding Identification of polyproline II regions derived from the proline-rich nuclear receptor coactivators PNRC and PNRC2: new insights for ERα coactivator interactions.The impact of either 4-R-hydroxyproline or 4-R-fluoroproline on the conformation and SH3m-cort binding of HPK1 proline-rich peptide.Arginine mimetics using α-guanidino acids: introduction of functional groups and stereochemistry adjacent to recognition guanidiniums in peptides Exploring the impact of polyproline II (PII) conformational bias on the binding of peptides to the SEM-5 SH3 domain.The effect of the polyproline II (PPII) conformation on the denatured state entropy.An electronic effect on protein structure.Neighboring residue effects in terminally blocked dipeptides: implications for residual secondary structures in intrinsically unfolded/disordered proteins.Osmotically induced helix-coil transition in poly(glutamic acid).A group 6 late embryogenesis abundant protein from common bean is a disordered protein with extended helical structure and oligomer-forming properties.Randomizing the unfolded state of peptides (and proteins) by nearest neighbor interactions between unlike residues.Elucidating Peptide and Protein Structure and Dynamics: UV Resonance Raman Spectroscopy.Effects of solvents on the intrinsic propensity of peptide backbone conformations.Molecular dynamics simulations of a new branched antimicrobial peptide: a comparison of force fields.Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of α-synuclein The Polarizable Atomic Multipole-based AMOEBA Force Field for Proteins.Sodium dodecyl sulfate monomers induce XAO peptide polyproline II to α-helix transition.Peptide Conformation Analysis Using an Integrated Bayesian Approach The polyproline II conformation in short alanine peptides is noncooperative Molecular recognition of protein surfaces: high affinity ligands for the CBP KIX domain.Intrinsic backbone preferences are fully present in blocked amino acids Strike a balance: optimization of backbone torsion parameters of AMBER polarizable force field for simulations of proteins and peptides.Further evidence for the absence of polyproline II stretch in the XAO peptide.Acidic-basic properties of three alanine-based peptides containing acidic and basic side chains: comparison between theory and experiment.Statistical coil model of the unfolded state: resolving the reconciliation problem.Building native protein conformation from highly approximate backbone torsion angles.Intermediacy of poly(L-proline) II and beta-strand conformations in poly(L-lysine) beta-sheet formation probed by temperature-jump/UV resonance Raman spectroscopy.Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides Quantitative determination of site-specific conformational distributions in an unfolded protein by solid-state nuclear magnetic resonance.Hydrogen-bond driven loop-closure kinetics in unfolded polypeptide chains.

P2860

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P2860

Polyproline II structure in a sequence of seven alanine residues.

http://www.wikidata.org/entity/Q34034318

description

2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年学术文章

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2002年学术文章

@zh-cn

2002年学术文章

@zh-hans

2002年学术文章

@zh-my

2002年学术文章

@zh-sg

2002年學術文章

@yue

name

Polyproline II structure in a sequence of seven alanine residues.

@ast

Polyproline II structure in a sequence of seven alanine residues.

@en

Polyproline II structure in a sequence of seven alanine residues.

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type

label

Polyproline II structure in a sequence of seven alanine residues.

@ast

Polyproline II structure in a sequence of seven alanine residues.

@en

Polyproline II structure in a sequence of seven alanine residues.

@nl

prefLabel

Polyproline II structure in a sequence of seven alanine residues.

@ast

Polyproline II structure in a sequence of seven alanine residues.

@en

Polyproline II structure in a sequence of seven alanine residues.

@nl

P1433

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P932

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Polyproline II structure in a sequence of seven alanine residues

@en

P2093

C Anders Olson

http://www.w3.org/2001/XMLSchema#string

George D Rose

http://www.w3.org/2001/XMLSchema#string

Neville R Kallenbach

http://www.w3.org/2001/XMLSchema#string

Robert L Baldwin

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution

Hydration structure of a collagen peptide

Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions

Phi/psi-chology: Ramachandran revisited

A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules

Solution structure and dynamics of biomolecules from Raman optical activity.

Vibrational circular dichroism spectroscopy of selected oligopeptide conformations.

The enthalpy of the alanine peptide helix measured by isothermal titration calorimetry using metal-binding to induce helix formation

Protein denaturation.

A survey of left-handed polyproline II helices

P304

9190-9195

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P31

scholarly article

P356

10.1073/PNAS.112193999

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P407

P433

14

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P478

99

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P50

Zhengshuang Shi

P577

2002-06-28T00:00:00Z

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P5875

11283413

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12091708

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123116

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