about
Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsecSolvation in protein folding analysis: Combination of theoretical and experimental approachesA molecular interpretation of 2D IR protein folding experiments with Markov state modelsSingle Molecule Analysis Research Tool (SMART): an integrated approach for analyzing single molecule dataThe effects of nonnative interactions on protein folding rates: theory and simulationProtein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after the structural collapseEvolution, energy landscapes and the paradoxes of protein folding.Investigation of protein folding by coarse-grained molecular dynamics with the UNRES force fieldNanosecond time-resolved polarization spectroscopies: tools for probing protein reaction mechanisms.Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.Energy landscape and multiroute folding of topologically complex proteins adenylate kinase and 2ouf-knotSpectroscopic studies of protein folding: linear and nonlinear methodsHigh-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.A microscopic view of miniprotein folding: enhanced folding efficiency through formation of an intermediate.Transient 2D IR spectroscopy of ubiquitin unfolding dynamicsTemperature-dependent downhill unfolding of ubiquitin. I. Nanosecond-to-millisecond resolved nonlinear infrared spectroscopy.Fast protein folding kineticsSingle-molecule Forster resonance energy transfer study of protein dynamics under denaturing conditions.What causes hyperfluorescence: folding intermediates or conformationally flexible native states?Variations in the fast folding rates of the lambda-repressor: a hybrid molecular dynamics study.Laser-driven microsecond temperature cycles analyzed by fluorescence polarization microscopy.Dynamics, energetics, and structure in protein foldingMaking connections between ultrafast protein folding kinetics and molecular dynamics simulations.Picosecond conformational transition and equilibration of a cyclic peptide.Investigation of routes and funnels in protein folding by free energy functional methods.Markov processes follow from the principle of maximum caliberMicrosecond folding dynamics of apomyoglobin at acidic pHTheoretical investigation of the photoinitiated folding of HP-36.Early events in protein folding explored by rapid mixing methods.Role of unfolded state heterogeneity and en-route ruggedness in protein folding kineticsSolvent-amino acid interaction energies in three-dimensional-lattice Monte Carlo simulations of a model 27-mer protein: Folding thermodynamics and kineticsMicrosecond folding experiments and simulations: a match is made.Principal component analysis for protein folding dynamicsThree-body interactions improve the prediction of rate and mechanism in protein folding models.First passage analysis of the folding of a β-sheet miniprotein: is it more realistic than the standard equilibrium approach?Kinetic definition of protein folding transition state ensembles and reaction coordinatesOptimized parameter selection reveals trends in Markov state models for protein folding.UV resonance Raman studies of the NaClO4 dependence of poly-L-lysine conformation and hydrogen exchange kinetics.Plasticity in the Oxidative Folding Pathway of the High Affinity Nerita Versicolor Carboxypeptidase Inhibitor (NvCI).Dynamic heterogeneity in the folding/unfolding transitions of FiP35.
P2860
Q24646211-21D57D46-6DE4-4CA3-8A3F-65DD2F95B5F2Q27643169-78D86181-7876-43A6-8606-08F4757ECBC4Q28660159-D22905DF-F27F-4581-B6C7-3F658AD2BB89Q28731931-08DCB99A-C090-4310-B781-3633132379BBQ30163987-9363F4D2-EF11-4784-A2EB-7035FBBB8B2DQ30167659-58772E7D-ABB6-439A-B74D-60A8108D3DF9Q30370011-BAFD80B0-76E9-4EF5-A9F5-A4A3886421B6Q30385785-8DC40F3C-2198-4A36-A8AE-7AEB72085A87Q30388775-F2214A18-BB47-4203-98C4-07E5661C4D8BQ30499610-51E86347-F445-47AA-A26D-78A59A167C85Q30528367-C1BCCA88-A355-414E-BD43-64BC00B0E805Q31042100-DDC23070-D1E4-4538-892A-952F08FD284EQ33215110-8ED70F1D-7CD4-499A-BF1C-DF74742D3AEFQ33226561-56C1192F-0918-4BFD-87CB-7955409C2938Q33286786-D9845A1A-4260-40C9-9F3B-A5E98580091AQ33326719-4FC538E3-06F7-49CA-943B-1B7B5CCEDCBBQ33719314-CB63E869-B946-4A81-8759-3D1C7C97EB30Q34098641-411299CF-CE2A-4FD1-AC72-A11297121AB6Q34178343-F740ED46-5A59-4A59-87E7-2BBC34F725ABQ34186231-6E53C2BD-5BC0-4125-87D3-CF6EE860486EQ34481571-0AD44F86-E910-4BF0-A427-6ABEC61EF4BEQ34546482-8F1752E8-C889-4B85-AE10-301FFE61D030Q34794973-C2E914F6-B5C0-453F-AE43-13F1F89F446FQ35143250-F0C6CFAC-0119-4532-8805-DC1DEBB5BC2DQ35779502-C1E75762-FB91-4FC2-8A00-F42214E2613DQ35798350-B02C4790-B0AE-4255-B9AB-21306543D626Q36344210-0AADB343-E548-4DE8-B4D0-15CA658054CCQ36458012-0C6A59A6-E49E-4F9F-B18D-7CB23A74824AQ36472801-DFE2266C-2BDF-4F98-8C27-7261A56F6A4EQ36474009-BBBD6C6A-88D5-417B-A293-2CEA6A593629Q36526437-166E59DE-2467-46F9-BD51-EC6B461F4290Q36784578-8C0DD403-7EFF-48DF-B314-1D2E329C5551Q37120734-C93F6901-B3B1-4195-A687-9962DB1749B5Q37589571-EBE1E35E-C3AD-4E78-B715-E6982FE0EB39Q37727675-7DAE4F51-0DC8-4513-9D64-167E719D8D3BQ39133279-E0203250-9009-44AB-8716-B39D03FCBD08Q39162913-67CC05E7-F64C-4870-86C1-92A561AA7913Q40685954-A9542B04-E438-4366-A08D-BE2712161FC5Q41020151-1B180EC8-FBD1-4DB2-8811-00550327177EQ41100545-43FC6440-0C7A-4648-81F9-3AB0BE21D3B1
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The fast protein folding problem.
@ast
The fast protein folding problem.
@en
type
label
The fast protein folding problem.
@ast
The fast protein folding problem.
@en
prefLabel
The fast protein folding problem.
@ast
The fast protein folding problem.
@en
P1476
The fast protein folding problem.
@en
P2093
Gruebele M
P304
P356
10.1146/ANNUREV.PHYSCHEM.50.1.485
P577
1999-01-01T00:00:00Z