about
Insights into protein aggregation by NMR characterization of insoluble SH3 mutants solubilized in salt-free waterMicrocanonical thermostatistics of coarse-grained proteins with amyloidogenic propensity.Robustness of atomistic Gō models in predicting native-like folding intermediates.The redundancy of NMR restraints can be used to accelerate the unfolding behavior of an SH3 domain during molecular dynamics simulationsThermodynamic features characterizing good and bad folding sequences obtained using a simplified off-lattice protein model.P versus Q: structural reaction coordinates capture protein folding on smooth landscapes.Geometric and physical considerations for realistic protein models.On the origin and highly likely completeness of single-domain protein structures.Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kineticsFold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Molecular simulations of cotranslational protein folding: fragment stabilities, folding cooperativity, and trapping in the ribosome.Analysis of the free-energy surface of proteins from reversible folding simulations.Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulationsHigh-resolution protein folding with a transferable potential.Why do protein folding rates correlate with metrics of native topology?Collapse kinetics and chevron plots from simulations of denaturant-dependent folding of globular proteins.Understanding ensemble protein folding at atomic detailProtein folding thermodynamics and dynamics: where physics, chemistry, and biology meet.Overview of protein folding mechanisms: experimental and theoretical approaches to probing energy landscapes.The loop hypothesis: contribution of early formed specific non-local interactions to the determination of protein folding pathways.Thermodynamics and kinetics of the hairpin ribozyme from atomistic folding/unfolding simulations.Toward a quantitative description of microscopic pathway heterogeneity in protein folding.The protein folding transition state: Insights from kinetics and thermodynamics
P2860
Q28471978-39EBE7EA-CA4F-434F-A821-8558FE214930Q30009951-07BE7DC9-43A6-4B74-B72F-74C7FC070AC6Q30010022-04A296A8-CF65-4E3F-A0A2-79EE49016BD7Q30010196-9FB66FC5-240A-4868-84C1-16030525862CQ30159682-3A96C475-A7C7-40CE-8CE7-1036C95C290DQ30159963-F052CFAD-C050-453D-B657-7263F32E62AAQ30351512-A45908F1-1B38-46DA-B700-A143389B60D6Q30352967-4CFB6F96-9DCA-4D56-A672-75B8E4363537Q30485479-4408399F-4528-48AF-9C1E-0D19BB77C873Q30691136-AB06B99C-90D4-46C9-B1E2-27AD49106E21Q33247451-69666151-CB09-4CA0-9BC1-17F07E7184FDQ33480934-95B2AADE-937C-4F69-BE6E-A37B7B168E02Q34022990-EF8E58C2-E6F2-4849-9F94-46C6405A559FQ34244862-CAB116F1-419F-4178-962F-F10D208B14C2Q34256511-EDE9E3D6-7638-401F-9324-73F411E6B9D8Q34977753-1C2DDAFC-85F4-42E8-85D4-B3DBA029B5D1Q35128687-244F2E5A-9FE5-458A-8523-DF3717DCFC24Q36472755-3F9BECD1-BBF4-4605-B30C-B31434ED0935Q37999300-DFC68FBA-D0FB-43DE-BA14-F65F1434EF65Q38783036-90A6B6BC-2925-49EC-9458-86FA3654CA11Q42362871-D6C4452E-CCA4-4FE1-BCDD-727B05AB9C9BQ47879093-CBA05A15-52CF-4A63-939D-97813154D9CFQ58658659-84597C0D-0E48-4FE5-AAE1-A1539E16696C
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Nucleation and the transition state of the SH3 domain.
@ast
Nucleation and the transition state of the SH3 domain.
@en
type
label
Nucleation and the transition state of the SH3 domain.
@ast
Nucleation and the transition state of the SH3 domain.
@en
prefLabel
Nucleation and the transition state of the SH3 domain.
@ast
Nucleation and the transition state of the SH3 domain.
@en
P1476
Nucleation and the transition state of the SH3 domain.
@en
P2093
Isaac A Hubner
Katherine A Edmonds
P304
P356
10.1016/J.JMB.2005.03.050
P407
P577
2005-04-13T00:00:00Z
P5875
P698
P818
q-bio/0503027