Multiple pathways on a protein-folding energy landscape: kinetic evidence.
about
The protein folding problemMechanism of protein folding.Nanosecond time-resolved polarization spectroscopies: tools for probing protein reaction mechanisms.Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.Kinetics of and intermediates in a photocycle branching reaction of the photoactive yellow protein from Ectothiorhodospira halophila.Protein folding and unfolding on a complex energy landscape.Heme ligation and conformational plasticity in the isolated c domain of cytochrome cd1 nitrite reductase.An estimate of the numbers and density of low-energy structures (or decoys) in the conformational landscape of proteins.Pump-Probe X-ray Solution Scattering Reveals Accelerated Folding of Cytochrome c Upon Suppression of MisligationOptimal use of data in parallel tempering simulations for the construction of discrete-state Markov models of biomolecular dynamics.alpha-helix formation: discontinuous molecular dynamics on an intermediate-resolution protein model.Laser desorption dual spray post-ionization mass spectrometry for direct analysis of samples via two informative channels.Conformational equilibration time of unfolded protein chains and the folding speed limit.Chiral vibrational structures of proteins at interfaces probed by sum frequency generation spectroscopy.Probing kinetic mechanisms of protein function and folding with time-resolved natural and magnetic chiroptical spectroscopiesTuning the Attempt Frequency of Protein Folding Dynamics via Transition-State Rigidification: Application to Trp-Cage.Investigation of routes and funnels in protein folding by free energy functional methods.Infrared spectroscopic discrimination between the loop and alpha-helices and determination of the loop diffusion kinetics by temperature-jump time-resolved infrared spectroscopy for cytochrome cCytochrome c folds through a smooth funnelConstructing the equilibrium ensemble of folding pathways from short off-equilibrium simulations.Probing early events in ferrous cytochrome c folding with time-resolved natural and magnetic circular dichroism spectroscopiesEarly events, kinetic intermediates and the mechanism of protein folding in cytochrome C.Effects of Congo red on aβ(1-40) fibril formation process and morphology.Characterization of equilibrium intermediates in denaturant-induced unfolding of ferrous and ferric cytochromes c using magnetic circular dichroism, circular dichroism, and optical absorption spectroscopies.The principle of stationary action in biophysics: stability in protein folding.Folding mechanism of reduced Cytochrome c: equilibrium and kinetic properties in the presence of carbon monoxide.Probing molecular kinetics with Markov models: metastable states, transition pathways and spectroscopic observables.Osmolytes induce structure in an early intermediate on the folding pathway of barstar.Disulfide driven folding for a conditionally disordered protein.Packing energetics determine the folding routes of the RNase-H proteins.
P2860
Q28284812-3B07B43C-ECAA-4A0C-9280-E60A1678ADF7Q30168709-704BBC59-1EFB-4670-97B9-E6CF39ACA5C1Q30388775-D601CE72-CDB8-4C81-8BBA-E3938B6B7C93Q30499610-265488F3-A25C-49D8-BA10-80079042850AQ30769471-F1955D5A-A366-4A31-986C-88E3677669B7Q30840310-29DE2A42-BB8C-4C9F-9325-5E67663C656BQ30943861-B86B8C8D-ABC1-4F34-AC8F-57185591E1D6Q33428558-40E0D0EE-AAF6-41CC-9E9E-9CE817364F61Q33811190-6923E2BB-677E-477D-9614-CFB0212DDE0BQ33948378-2E3E356D-5C17-41BF-93D6-9AE9D623836DQ34084053-BADBFED4-FF99-40EC-9438-6DC392AB7358Q34573381-2F8628EA-790C-4EAB-A55F-73FF952715DEQ35082991-236F9EFD-9DDB-421F-9974-EFFCE3531D7CQ35669573-064FDC26-876D-4AE3-9B40-8E12B3A3E658Q35719441-DEC99B58-B867-4C6F-B1F6-4EC3F9BAEDA7Q35776121-EC4871FD-C6CC-4D0F-927A-C086F8139EDCQ35779502-23F13D4D-2E80-4CE6-8D5A-B883E683BC2DQ36008707-F778048E-7EF1-4755-AEB4-7A6FE6DA355CQ36281933-83D1759E-B6A5-4A6C-B907-CB840195DE3BQ37410885-1589467F-E28E-430E-A1C7-8DA3FD809BE5Q37439424-7EEA9F24-804D-4999-A929-1174FD1D20C7Q37495427-495A1963-AE2E-492D-81F3-DD73A1E53876Q39287470-4F003F28-4979-4D1B-B6E2-F87538694667Q41720044-1E0C9909-2754-4255-AA87-15A0004CD936Q41866163-60C8508A-D743-40F1-8ED6-CE5C53D80B5EQ42079488-0877B999-032F-4E5B-88A3-77CB160221D8Q43699792-B09BA81F-2A2F-4A69-812D-3E326F3DD5AAQ44982138-B9A69E2C-A650-43FE-AA48-84ECA6E16013Q47112353-ED80F1DA-0776-4341-92E9-55B6FCB01499Q48104918-21714867-F159-44E1-9340-74EB280DE1A2
P2860
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին 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
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@ast
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@en
type
label
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@ast
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@en
prefLabel
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@ast
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@en
P2093
P2860
P356
P1476
Multiple pathways on a protein-folding energy landscape: kinetic evidence.
@en
P2093
D S Kliger
R A Goldbeck
R M Esquerra
Y G Thomas
P2860
P304
P356
10.1073/PNAS.96.6.2782
P407
P577
1999-03-01T00:00:00Z