Nature of the charged-group effect on the stability of the C-peptide helix. - Wikidata - awgldk - TriplyDB

Nature of the charged-group effect on the stability of the C-peptide helix.

Nature of the charged-group effect on the stability of the C-peptide helix.

http://www.wikidata.org/entity/Q37684326

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Translating Koch's postulates to identify matrix metalloproteinase roles in postmyocardial infarction remodeling: cardiac metalloproteinase actions (CarMA) postulates Novel lynx spider toxin shares common molecular architecture with defense peptides from frog skin Folding of beta pep-4 beta-sheet sandwich dimers and tetramers is influenced by aliphatic hydrophobic residues at the intersubunit interface Force Field for Peptides and Proteins based on the Classical Drude Oscillator Testing the Coulomb/Accessible Surface Area solvent model for protein stability, ligand binding, and protein design.Alpha-helix stabilization by natural and unnatural amino acids with alkyl side chains.Proposed structure of putative glucose channel in GLUT1 facilitative glucose transporter.Helix-stabilizing effects of the pentapeptide KIFMK and its related peptides on the sodium channel inactivation gate peptides.Molecular dynamics of the structural changes of helical peptides induced by pressure.Checkpoint kinase ATR promotes nucleotide excision repair of UV-induced DNA damage via physical interaction with xeroderma pigmentosum group A.Determination of lysine pK values using [5-13C]lysine: application to the lyase domain of DNA Pol beta.Protein fragments as probes in the study of protein folding mechanisms: differential effects of dihydrofolate reductase fragments on the refolding of the intact protein.Constant pH replica exchange molecular dynamics in biomolecules using a discrete protonation model Role of backbone hydration and salt-bridge formation in stability of alpha-helix in solution.Unusually stable helix formation in short alanine-based peptides Effect of urea on peptide conformation in water: molecular dynamics and experimental characterization.Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design.The N-terminal helix controls the transition between the soluble and amyloid states of an FF domain Exploring atomistic details of pH-dependent peptide folding Constant pH molecular dynamics of proteins in explicit solvent with proton tautomerism.High-resolution crystal structures of protein helices reconciled with three-centered hydrogen bonds and multipole electrostatics.Current status of protein force fields for molecular dynamics simulations.The amyloid precursor protein copper binding domain histidine residues 149 and 151 mediate APP stability and metabolism.Protein folding dynamics: the diffusion-collision model and experimental data.Strategies and rationales for the de novo design of a helical hairpin peptide A recipe for designing water-soluble, beta-sheet-forming peptides.Testing the diffusing boundary model for the helix-coil transition in peptides The intrinsic helix-forming tendency of L-alanine.pH-replica exchange molecular dynamics in proteins using a discrete protonation method.Effect of side chain-backbone electrostatic interactions on the stability of alpha-helices.Crystallographic structure of an active, sequence-engineered ribonuclease.Design of Stable α-Helical Peptides and Thermostable Proteins in Biotechnology and Biomedicine.How force unfolding differs from chemical denaturation.Emerging approaches in the molecular design of receptor-selective peptide ligands: conformational, topographical and dynamic considerations.Can a polyproline II helical motif be used in the context of sequence-selective major groove recognition of B-DNA? A molecular modelling investigation.Grid-based backbone correction to the ff12SB protein force field for implicit-solvent simulations New stochastic strategy to analyze helix folding.Effects of charge states, charge sites and side chain interactions on conformational preferences of a series of model peptide ions.Local interactions in protein folding: lessons from the alpha-helix.Multiple native-like conformations trapped via self-association-induced hydrophobic collapse of the 33-residue beta-sheet domain from platelet factor 4.

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P2860

Nature of the charged-group effect on the stability of the C-peptide helix.

http://www.wikidata.org/entity/Q37684326

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on April 1985

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Nature of the charged-group effect on the stability of the C-peptide helix.

@en

Nature of the charged-group effect on the stability of the C-peptide helix.

@nl

type

label

Nature of the charged-group effect on the stability of the C-peptide helix.

@en

Nature of the charged-group effect on the stability of the C-peptide helix.

@nl

prefLabel

Nature of the charged-group effect on the stability of the C-peptide helix.

@en

Nature of the charged-group effect on the stability of the C-peptide helix.

@nl

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

P1476

Nature of the charged-group effect on the stability of the C-peptide helix.

@en

P2093

D N Brems

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

E J York

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

I M Chaiken

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

J M Stewart

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

K R Shoemaker

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

P S Kim

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

R L Baldwin

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

S Marqusee

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

P2860

Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins

The alpha-helix as an electric macro-dipole.

A salt bridge stabilizes the helix formed by isolated C-peptide of RNase A

alpha-Helix dipole model and electrostatic stabilization of 4-alpha-helical proteins.

A competing salt-bridge suppresses helix formation by the isolated C-peptide carboxylate of ribonuclease A.

The alpha-helix dipole and the properties of proteins.

Electrostatic interactions in globular proteins. Different dielectric models applied to the packing of alpha-helices

P304

2349-2353

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scholarly article

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10.1073/PNAS.82.8.2349

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P433

8

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82

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1985-04-01T00:00:00Z

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19303524

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P698

3857585

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397555

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