Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
about
The Trp-cage: optimizing the stability of a globular miniproteinEngineering a two-helix bundle protein for folding studiesThe protein folding problemEstimation of protein folding free energy barriers from calorimetric data by multi-model Bayesian analysis.Understanding protein folding cooperativity based on topological consideration.Multidimensional theory of protein folding.Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in waterThe folding of a family of three-helix bundle proteins: spectrin R15 has a robust folding nucleus, unlike its homologous neighbours.Distinguishing between cooperative and unimodal downhill protein folding.Direct observation of barrier-limited folding of BBL by single-molecule fluorescence resonance energy transfer.Folding simulations of a de novo designed protein with a betaalphabeta fold.Fast protein folding kineticsThe folding energy landscape and free energy excitations of cytochrome cGeneral structural motifs of amyloid protofilaments.Elucidation of the interaction loci of the human pyruvate dehydrogenase complex E2·E3BP core with pyruvate dehydrogenase kinase 1 and kinase 2 by H/D exchange mass spectrometry and nuclear magnetic resonanceObservation of two families of folding pathways of BBL.Site-specific collapse dynamics guide the formation of the cytochrome c' four-helix bundle.Effects of two solvent conditions on the free energy landscape of the BBL peripheral subunit binding domainProtein folding of the SAP domain, a naturally occurring two-helix bundle.Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulationInteraction Networks in Protein Folding via Atomic-Resolution Experiments and Long-Time-Scale Molecular Dynamics SimulationsOrigins of barriers and barrierless folding in BBL.Cooperative folding kinetics of BBL protein and peripheral subunit-binding domain homologues.Observation of noncooperative folding thermodynamics in simulations of 1BBL.Intermediates: ubiquitous species on folding energy landscapes?Mutational effects on the folding dynamics of a minimized hairpin.Using VIPT-jump to distinguish between different folding mechanisms: application to BBL and a Trpzip.Dynamics of one-state downhill protein folding.Direct observation of ultrafast folding and denatured state dynamics in single protein molecules.What lessons can be learned from studying the folding of homologous proteins?Nuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.How cooperative are protein folding and unfolding transitions?Different members of a simple three-helix bundle protein family have very different folding rate constants and fold by different mechanismsPhi-value analysis for ultrafast folding proteins by NMR relaxation dispersion.Kinetic and thermodynamic studies reveal chemokine homologues CC11 and CC24 with an almost identical tertiary structure have different folding pathways.The human peripheral subunit-binding domain folds rapidly while overcoming repulsive Coulomb forces.Protein folding kinetics: barrier effects in chemical and thermal denaturation experiments.Protein unfolding rates correlate as strongly as folding rates with native structure.How general is the nucleation-condensation mechanism?Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein
P2860
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P2860
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
description
2005 nî lūn-bûn
@nan
2005 թվականի հոկտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@en
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@nl
type
label
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@en
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@nl
prefLabel
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@en
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@nl
P2093
P1476
Ultra-fast barrier-limited folding in the peripheral subunit-binding domain family.
@en
P2093
Christopher M Johnson
Mark D Allen
Neil Ferguson
Pamela J Schartau
Satoshi Sato
Timothy D Sharpe
Trevor J Rutherford
P304
P356
10.1016/J.JMB.2005.08.031
P407
P50
P577
2005-10-01T00:00:00Z