Understanding the key factors that control the rate of beta-hairpin folding. - Wikidata - wikimedia - TriplyDB

Understanding the key factors that control the rate of beta-hairpin folding.

Understanding the key factors that control the rate of beta-hairpin folding.

http://www.wikidata.org/entity/Q37619359

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Folding very short peptides using molecular dynamics Balancing solvation and intramolecular interactions: toward a consistent generalized Born force field Combinatorial pattern discovery approach for the folding trajectory analysis of a beta-hairpin.Structure and Flexibility of the Complete Periplasmic Domain of BamA: The Protein Insertion Machine of the Outer Membrane Circular Permutation of a WW Domain: Folding Still Occurs after Excising the Turn of the Folding-Nucleating Hairpin Folding of proteins with an all-atom Go-model.Similarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulations Transient two-dimensional IR spectrometer for probing nanosecond temperature-jump kinetics.Spectroscopic studies of protein folding: linear and nonlinear methods The effect of charge-charge interactions on the kinetics of alpha-helix formation.Coherent multidimensional vibrational spectroscopy of biomolecules: concepts, simulations, and challenges.Flow-induced beta-hairpin folding of the glycoprotein Ibalpha beta-switch The interplay of turn formation and hydrophobic interactions on the early kinetic events in protein folding.Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.Hairpin folding rates reflect mutations within and remote from the turn region.Infrared study of the folding mechanism of a helical hairpin: porcine PYY.Folding of a heterogeneous β-hairpin peptide from temperature-jump 2D IR spectroscopy.Microscopic events in β-hairpin folding from alternative unfolded ensembles Tightening up the structure, lighting up the pathway: Application of molecular constraints and light to manipulate protein folding, self-assembly and function.β-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins.Two-dimensional vibrational optical probes for peptide fast folding investigation.Local structure of beta-hairpin isotopomers by FTIR, 2D IR, and ab initio theory Using thioamides to site-specifically interrogate the dynamics of hydrogen bond formation in β-sheet folding.Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formation Predicting the folding pathway of engrailed homeodomain with a probabilistic roadmap enhanced reaction-path algorithm UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding.High temperature unfolding simulations of the TRPZ1 peptide.Mutational effects on the folding dynamics of a minimized hairpin.Combining coarse-grained protein models with replica-exchange all-atom molecular dynamics.Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip.Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.Roles of beta-turns in protein folding: from peptide models to protein engineering.Very short peptides with stable folds: building on the interrelationship of Trp/Trp, Trp/cation, and Trp/backbone-amide interaction geometries.Multiscale implementation of infinite-swap replica exchange molecular dynamics.Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly.Folding mechanism of β-hairpin trpzip2: heterogeneity, transition state and folding pathways.How quickly can a β-hairpin fold from its transition state?The sensitivity of folding free energy landscapes of trpzips to mutations in the hydrophobic core.Light-Switchable Peptides with a Hemithioindigo Unit: Peptide Design, Photochromism, and Optical Spectroscopy.

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P2860

Understanding the key factors that control the rate of beta-hairpin folding.

http://www.wikidata.org/entity/Q37619359

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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2004年學術文章

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name

Understanding the key factors that control the rate of beta-hairpin folding.

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Understanding the key factors that control the rate of beta-hairpin folding.

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type

label

Understanding the key factors that control the rate of beta-hairpin folding.

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Understanding the key factors that control the rate of beta-hairpin folding.

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prefLabel

Understanding the key factors that control the rate of beta-hairpin folding.

@en

Understanding the key factors that control the rate of beta-hairpin folding.

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

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Understanding the key factors that control the rate of beta-hairpin folding.

@en

P2093

Cheng-Yen Huang

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

Deguo Du

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Feng Gai

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

Yongjin Zhu

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P2860

Tryptophan zippers: Stable, monomeric -hairpins

A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G

Mapping the transition state and pathway of protein folding by protein engineering

Turns in peptides and proteins

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

Stiffness of the distal loop restricts the structural heterogeneity of the transition state ensemble in SH3 domains.

Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchange

Measuring the refolding of beta-sheets with different turn sequences on a nanosecond time scale.

The free energy landscape for beta hairpin folding in explicit water.

Helix formation via conformation diffusion search

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