about
Fast and faster: a designed variant of the B-domain of protein A folds in 3 microsecPolymer principles and protein foldingUsing flexible loop mimetics to extend -value analysis to secondary structure interactionsStructural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics.Crystal structures of engrailed homeodomain mutants: implications for stability and dynamicsRapid Folding and Unfolding of Apaf-1 CARDEngineering a two-helix bundle protein for folding studiesA Survey of λ Repressor Fragments from Two-State to Downhill FoldingObligatory steps in protein folding and the conformational diversity of the transition stateFast-folding proteins under stressQuantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemesFolding propensities of synthetic peptide fragments covering the entire sequence of phage 434 Cro protein.Cytochrome c' folding triggered by electron transfer: fast and slow formation of four-helix bundlesA quantitative, high-throughput screen for protein stability.Distinguishing between cooperative and unimodal downhill protein folding.Microsecond folding dynamics of the F13W G29A mutant of the B domain of staphylococcal protein A by laser-induced temperature jump.Accuracy of SUPREX (stability of unpurified proteins from rates of H/D exchange) and MALDI mass spectrometry-derived protein unfolding free energies determined under non-EX2 exchange conditions.Slowing down downhill folding: a three-probe study.Analysis of the free-energy surface of proteins from reversible folding simulations.Fast protein folding kineticsElementary steps in protein folding.Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications.Submillisecond events in protein foldingHairpin folding rates reflect mutations within and remote from the turn region.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.Folding lambda-repressor at its speed limit.Probing the kinetics of single molecule protein folding.Ultrafast folding of alpha3D: a de novo designed three-helix bundle proteinMaking connections between ultrafast protein folding kinetics and molecular dynamics simulations.Meeting halfway on the bridge between protein folding theory and experiment.Folding pathway of a lattice model for proteins.Protein folding and unfolding in microseconds to nanoseconds by experiment and simulationProtein topology determines binding mechanism.Configuration-dependent diffusion can shift the kinetic transition state and barrier height of protein foldingStructural Characterization of λ-Repressor Folding from All-Atom Molecular Dynamics SimulationsDiffusion control in an elementary protein folding reaction.Mutational analysis of the BPTI folding pathway: I. Effects of aromatic-->leucine substitutions on the distribution of folding intermediatesThe alpha-helix folds on the millisecond time scale.Solvent-tuning the collapse and helix formation time scales of lambda(6-85)*.
P2860
Q24646211-94D72FDA-BE62-4577-8B41-7C3C78628B6AQ24672635-948FC269-2DA1-4CFB-A744-F6CC16700061Q27635868-86F0672E-5558-4455-9828-E7E61A69959AQ27639890-D4E56A66-C5F5-4CC2-9332-4A4C7A48DCD1Q27641843-A27A426A-678B-4B45-8EE3-449B76731B25Q27644353-1A74F361-DC5E-46D2-B619-3C3576AFB416Q27659490-C81F5EC1-363D-4E7D-B936-C21ED7C97A00Q27659628-74456912-9ADA-42FB-8E0C-C259A1F2F274Q27765097-2AD42547-604C-4F6A-AD43-1788D871BF6BQ28083935-40BE38FB-A09E-4D17-9914-00283FFA830FQ28833810-49376AD9-65A3-4360-8B57-85B5A1D99283Q30580694-8CC0033A-4959-404C-9CAF-30885E8F5729Q30686772-9D0D7DE8-5C00-4E34-A81D-A62E4593AE4DQ30885030-856E99B1-3F31-4CBF-886D-B35C082AAADCQ31089493-F2579A5C-B49B-4C5B-A4CF-4152D9870C97Q33199062-DC4EA50D-778B-40BF-8D6E-EA3866D84910Q33252060-61D46E0F-D7DA-4925-92A2-45C3136F8B1CQ33478772-D4135B86-9D29-44E8-8698-A898C96DE36BQ33480934-7639F295-F980-44E1-A4F4-32CE0A29A92BQ33719314-3A83144F-97DC-4DB4-B49E-769393D65BE6Q33737296-DB7BE908-4012-447E-A8DF-CE3B6C98DB94Q33739669-61866A8C-E105-4863-A1D9-CC9E7CC997CBQ33793412-64BAC6E2-4929-429F-B981-B65395ADB42FQ34098386-A7241EFD-1EBF-481B-B001-18490ECA802EQ34178343-16B7D216-E0BB-4F8A-976B-E1B5BAC283F7Q34186231-9264C040-C1CC-4D37-B2C1-4DDBD80FEAA1Q34186340-8FD5DE40-73E4-44C0-BD77-5C281CFBDDACQ34187969-55B714EA-EA34-4BE9-9282-AD76BF281A53Q34788483-0F6D35C5-9D76-454C-9B41-75E0F5F1B6E3Q34794973-F19F8BB3-86BA-4DF7-AF59-14AA4220A3D9Q34913657-0C51E314-D792-4C69-9BC5-E1884E941B16Q34987137-96EDB6FF-2459-4300-809A-215F3D765FF8Q35566520-BFF10DF5-B0AF-4497-957A-F8A6E55E59D3Q35734060-2EE0A5B5-E614-4FE5-A759-6F7B4ED054F1Q35990251-246AD3EC-3D29-424C-A6A4-7DF3B58F76BAQ36039378-98D1EC6B-96A5-467B-8840-DA3AA9533257Q36153029-C7A6E8A3-70EC-4D09-B074-44ADB8C812DCQ36280455-D905FA28-BE0A-4310-A1AA-A5C40250CC4BQ36392031-CC2FDF2D-9D2F-40C9-9E1C-6333F7B79395Q36458076-20B5F206-5854-47DC-8275-162C312D0687
P2860
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Submillisecond folding of monomeric lambda repressor
@ast
Submillisecond folding of monomeric lambda repressor
@en
Submillisecond folding of monomeric lambda repressor
@nl
type
label
Submillisecond folding of monomeric lambda repressor
@ast
Submillisecond folding of monomeric lambda repressor
@en
Submillisecond folding of monomeric lambda repressor
@nl
prefLabel
Submillisecond folding of monomeric lambda repressor
@ast
Submillisecond folding of monomeric lambda repressor
@en
Submillisecond folding of monomeric lambda repressor
@nl
P2860
P356
P1476
Submillisecond folding of monomeric lambda repressor
@en
P2093
P2860
P304
P356
10.1073/PNAS.92.15.6878
P407
P577
1995-07-01T00:00:00Z