about
The helix turn helix motif as an ultrafast independently folding domain: The pathway of folding of Engrailed homeodomainTwist-open mechanism of DNA damage recognition by the Rad4/XPC nucleotide excision repair complexSlow proton transfer coupled to unfolding explains the puzzling results of single-molecule experiments on BBL, a paradigmatic downhill folding proteinDe novo prediction of protein folding pathways and structure using the principle of sequential stabilizationForce-dependent switch in protein unfolding pathways and transition-state movements.Better biomolecule thermodynamics from kinetics.Nonequilibrium dynamics of helix reorganization observed by transient 2D IR spectroscopy.Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.Transient two-dimensional IR spectrometer for probing nanosecond temperature-jump kinetics.How fast is protein hydrophobic collapse?Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.Transient 2D IR spectroscopy of ubiquitin unfolding dynamicsTemperature-dependent downhill unfolding of ubiquitin. I. Nanosecond-to-millisecond resolved nonlinear infrared spectroscopy.Analysis of the free-energy surface of proteins from reversible folding simulations.Single-molecule fluorescence probes dynamics of barrier crossing.Exploring protein-folding ensembles: a variable-barrier model for the analysis of equilibrium unfolding experiments.Coordinate-dependent diffusion in protein folding.Fast protein folding kineticsKinetics are probe-dependent during downhill folding of an engineered lambda6-85 protein.Alpha-helix formation in a photoswitchable peptide tracked from picoseconds to microseconds by time-resolved IR spectroscopy.Entropy rectifies the Brownian steps of kinesin.Protein folding by distributed computing and the denatured state ensemble.Common intermediates and kinetics, but different energetics, in the assembly of SNARE proteins.How fast-folding proteins fold.Single reconstituted neuronal SNARE complexes zipper in three distinct stages.Atom-by-atom analysis of global downhill protein folding.Temperature and voltage coupling to channel opening in transient receptor potential melastatin 8 (TRPM8).Ultrafast folding of alpha3D: a de novo designed three-helix bundle proteinReaching the protein folding speed limit with large, sub-microsecond pressure jumps.The binding mechanisms of intrinsically disordered proteins.Microscopic events in β-hairpin folding from alternative unfolded ensemblesDirect quantification of the attempt frequency determining the mechanical unfolding of ubiquitin proteinProteome folding kinetics is limited by protein halflife.A PDZ domain recapitulates a unifying mechanism for protein foldingHighly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.Loop formation in unfolded polypeptide chains on the picoseconds to microseconds time scale.Energy landscape of the reactions governing the Na+ deeply occluded state of the Na+/K+-ATPase in the giant axon of the Humboldt squidExploring one-state downhill protein folding in single molecules.Ultrafast dynamics of protein collapse from single-molecule photon statistics.β-Bulge triggers route-switching on the functional landscape of interleukin-1β.
P2860
Q27644846-FEA4C08B-4301-4BE2-9158-151FF55B7AB1Q27938970-6DB6B156-67CF-4A77-89A0-EB59B4B35970Q28534668-D457F9CF-2456-4019-ADE6-5126EEAB8774Q28714217-CA7E634B-C815-493B-AE12-C0D69C46B746Q30009030-7D831C49-0DA0-4659-BDBF-85064E9D7AC6Q30010275-863133DA-9515-4FF7-A08A-6EB51DDE49C6Q30447592-9CF5FB08-5395-4B0D-B4B0-E33D5E05E42AQ30499610-0C6843D3-DBA3-4281-AD29-EC1F01BF2479Q30832490-97F9D844-04C9-4424-B23B-1CE8C36163EDQ33193707-7666BA65-580F-4619-8A48-9ADFAB214C31Q33199062-4131F4E0-DAE9-4D10-9C16-DB6EC90D06EEQ33286786-BD0382DD-5CC7-4561-B685-4AFF1E9BA125Q33326719-BC15499E-2F51-4C9F-941D-0B943FC7145EQ33480934-6DE2D519-752C-468E-9F1E-A63040CDB927Q33565764-E93DEAF7-D9DC-4DDC-B269-EDD7A15C700DQ33580648-A43784B7-1941-4D77-A037-89BCAF037012Q33667020-5AF4E44E-6B61-4E30-9A46-42DA90798D41Q33719314-16367EBC-2E36-41E4-B53A-F1F3C287E0CBQ33850048-F3AF1EEC-DEAC-48A6-862E-4F118DB97230Q33850091-D05421ED-73F5-45C4-965A-DA5B64AA4A9DQ33992868-6D27586C-558B-4F2D-B65C-D160D4FD443BQ34133291-0266104F-A0CC-405A-BDE7-1125F7737D3FQ34196813-139D4EE4-3436-48E8-A11B-2489F5FFA7EFQ34228223-9F47A4AD-250B-4907-971B-BE5385A9D9ACQ34294781-F6FBAF15-24FD-4B81-9BBE-8FFA87BBF3A3Q34541834-9F27542F-47C7-4A0A-A856-BC5725BF683EQ34737973-F0F0E7BA-C257-4CB0-9368-E411CBF798B1Q34788483-60D00968-0D67-4E62-AF86-19927B932CBEQ34984103-D38DDAC0-F8AB-4088-BBA5-9175703E2CF7Q35062460-A97CFEFC-42F8-43F4-BB26-6A334020DAF9Q35090961-61925164-537D-4742-A805-B1AE54A0A5B9Q35213109-6C9DBDF2-AF30-43A6-A11C-B8AD89A339E3Q35418171-FD76F39E-81B9-4EC6-98F9-A9368EBE62DBQ35575881-4A7D8869-D60F-4439-B652-739892102579Q35590129-29F12304-EA2D-4F2A-B6E3-0352E9671352Q35629113-981C5E47-B332-45D4-AE8F-4BEEC55BF2D6Q35651403-4ECD5EAB-CB41-474C-910F-B2A7648077B8Q35657817-8D80680E-C022-4656-A3F9-E35994003154Q35669661-C43F8D8D-2CAA-4468-AF6B-A090DA8B412BQ35749603-7991F502-D8FB-4F0B-9834-B7E9358CB4C5
P2860
description
article publié dans la revue scientifique Nature
@fr
scientific article published in Nature
@en
wetenschappelijk artikel
@nl
наукова стаття, опублікована в Nature в травні 2003
@uk
name
Folding at the speed limit
@en
Folding at the speed limit
@nl
type
label
Folding at the speed limit
@en
Folding at the speed limit
@nl
prefLabel
Folding at the speed limit
@en
Folding at the speed limit
@nl
P2860
P356
P1433
P1476
Folding at the speed limit
@en
P2093
Martin Gruebele
Wei Yuan Yang
P2860
P2888
P304
P356
10.1038/NATURE01609
P407
P577
2003-05-01T00:00:00Z
P6179
1034007549