Hairpin folding rates reflect mutations within and remote from the turn region. - Wikidata - wikimedia - TriplyDB

Hairpin folding rates reflect mutations within and remote from the turn region.

Hairpin folding rates reflect mutations within and remote from the turn region.

http://www.wikidata.org/entity/Q34098386

about

The Trp-cage: optimizing the stability of a globular miniprotein Circular Permutation of a WW Domain: Folding Still Occurs after Excising the Turn of the Folding-Nucleating Hairpin An improved capping unit for stabilizing the ends of associated β-strands.Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in water Solution state structures of human pancreatic amylin and pramlintide.Stabilizing capping motif for beta-hairpins and sheets.beta-hairpin-forming peptides; models of early stages of protein folding.Captides: rigid junctions between beta sheets and small molecules.Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.Folding dynamics and pathways of the trp-cage miniproteins.Free-energy landscape of the GB1 hairpin in all-atom explicit solvent simulations with different force fields: Similarities and differences Microscopic events in β-hairpin folding from alternative unfolded ensembles β-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins.Thermodynamics of protein folding using a modified Wako-Saitô-Muñoz-Eaton model Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.Further optimization of a hybrid united-atom and coarse-grained force field for folding simulations: Improved backbone hydration and interactions between charged side chains.Mutational effects on the folding dynamics of a minimized hairpin.PRIMO: A Transferable Coarse-grained Force Field for Proteins.Very short peptides with stable folds: building on the interrelationship of Trp/Trp, Trp/cation, and Trp/backbone-amide interaction geometries.How quickly can a β-hairpin fold from its transition state?Minimization and optimization of designed beta-hairpin folds Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.The sensitivity of folding free energy landscapes of trpzips to mutations in the hydrophobic core.Optimization of a β-sheet-cap for long loop closure.Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization.A Structuring Repeat for Peptide Design: Long Beta Ribbons.Folding thermodynamics of β-hairpins studied by replica-exchange molecular dynamics simulations.Protein GB1 folding and assembly from structural elements.Terminal sidechain packing of a designed beta-hairpin influences conformation and stability.Molecular dynamics simulation indicating cold denaturation of β-hairpins.The universality of β-hairpin misfolding indicated by molecular dynamics simulations.Focused conformational sampling in proteins.13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.Structural features and molecular aggregations of designed triple-stranded β-sheets in single crystals.Decoding the energy landscape: extracting structure, dynamics and thermodynamics.Amide I two-dimensional infrared spectroscopy of β-hairpin peptides

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P2860

Hairpin folding rates reflect mutations within and remote from the turn region.

http://www.wikidata.org/entity/Q34098386

description

2005 nî lūn-bûn

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2005 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2005 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Hairpin folding rates reflect mutations within and remote from the turn region.

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Hairpin folding rates reflect mutations within and remote from the turn region.

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Hairpin folding rates reflect mutations within and remote from the turn region.

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type

label

Hairpin folding rates reflect mutations within and remote from the turn region.

@ast

Hairpin folding rates reflect mutations within and remote from the turn region.

@en

Hairpin folding rates reflect mutations within and remote from the turn region.

@nl

prefLabel

Hairpin folding rates reflect mutations within and remote from the turn region.

@ast

Hairpin folding rates reflect mutations within and remote from the turn region.

@en

Hairpin folding rates reflect mutations within and remote from the turn region.

@nl

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PNAS.0504392102

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

P1476

Hairpin folding rates reflect mutations within and remote from the turn region.

@en

P2093

James M Stewart

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

Katherine A Olsen

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

Niels H Andersen

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

R Matthew Fesinmeyer

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P2860

Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

Tryptophan zippers: Stable, monomeric -hairpins

Accurate computer-based design of a new backbone conformation in the second turn of protein L

Turn stability in β-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns

Computer-based redesign of a protein folding pathway

A short linear peptide that folds into a native stable beta-hairpin in aqueous solution

Fast kinetics and mechanisms in protein folding.

Enhanced hairpin stability through loop design: the case of the protein G B1 domain hairpin.

Nanosecond temperature jump relaxation dynamics of cyclic beta-hairpin peptides.

Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin.

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15483-15487

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scholarly article

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10.1073/PNAS.0504392102

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43

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102

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2005-10-14T00:00:00Z

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16227442

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1266093

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