about
Using deeply trapped intermediates to map the cytochrome c folding landscapeDNA binding properties of the small cascade subunit Csa5The dual role of a loop with low loop contact distance in folding and domain swapping.Toward resolution of ambiguity for the unfolded state.Direct visualization reveals dynamics of a transient intermediate during protein assembly.Ribosylation rapidly induces alpha-synuclein to form highly cytotoxic molten globules of advanced glycation end products.Towards understanding the mechanisms of molecular recognition by computer simulations of ligand-protein interactions.Folding thermodynamics of model four-strand antiparallel beta-sheet proteins.Protein folding pathways and kinetics: molecular dynamics simulations of beta-strand motifs.Assembly and kinetic folding pathways of a tetrameric beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein modelsDefective protein folding and aggregation as the basis of neurodegenerative diseases: the darker aspect of proteins.Meeting halfway on the bridge between protein folding theory and experiment.Folding pathway of a lattice model for proteins.What is the role of non-native intermediates of beta-lactoglobulin in protein folding?Intermediates can accelerate protein folding.Single-molecule fluorescence studies of protein folding and conformational dynamicsDirect observation of an ensemble of stable collapsed states in the mechanical folding of ubiquitin.Conformation and thermodynamic stability of pre-molten and molten globule states of mammalian cytochromes-c.Progress in the de novo design of structured peptoid protein mimics.Detecting selection on protein stability through statistical mechanical models of folding and evolutionThe human alpha-lactalbumin molten globule: comparison of structural preferences at pH 2 and pH 7.Kinetic Analysis of Guanidine Hydrochloride Inactivation of β-Galactosidase in the Presence of Galactose.Thermodynamics and stability of a beta-sheet complex: molecular dynamics simulations on simplified off-lattice protein models.The structure of denatured alpha-lactalbumin elucidated by the technique of disulfide scrambling: fractionation of conformational isomers of alpha-lactalbumin.The unfolding mechanism and the disulfide structures of denatured lysozyme.Role of hydrophilic and hydrophobic contacts in folding of the second beta-hairpin fragment of protein G: molecular dynamics simulation studies of an all-atom model.A new concept for molecular engineering of artificial enzymes: a multiscale simulation.Effect of non-specific interactions on formation and stability of specific complexes.Topology-based potentials and the study of the competition between protein folding and aggregation.Influence of the chain stiffness on the thermodynamics of a Gō-type model for protein folding.Thermodynamics of Go-type models for protein folding.The role of sidechain packing and native contact interactions in folding: Discontinuous molecular dynamics folding simulations of an all-atom Gō model of fragment B of Staphylococcal protein AA simple simulation model can reproduce the thermodynamic folding intermediate of apoflavodoxin
P2860
Q27639259-EAB7514A-75BC-439E-ACAF-CF0C7B3049E4Q28542520-CBC12D04-FBE8-428E-B46D-86E372FE5885Q30165352-730849D1-14EF-4620-B514-3CDE916823AEQ30369370-4AED8069-B803-4191-8F5B-C53CEACB62F0Q30499803-0CB172DC-9999-409E-A719-410283E1E028Q33530116-93063910-71B9-4783-96F4-D361C444453EQ33803957-05A2F744-3430-4516-9E41-AEA0C29BD683Q34177130-6D30F7D9-7D68-41BB-91B3-E008581C4347Q34178469-410990C4-75B1-4E56-A089-2B35FE6D19BEQ34184303-7B3FA883-C061-4D7E-95A4-04FEBB135FC9Q34185176-9893A160-AF16-453A-B3D1-CD0DDEA415E4Q34913657-105CC920-94E4-4D7D-B17F-AFD2F75C67A5Q34987137-2629C63F-B5BA-4872-9FDB-569756082A9CQ35839822-364B1C78-1C34-4E2B-9208-3BFFC5EDD16EQ36379246-746B57A9-C29F-4EFA-8594-3666CCB77CDBQ36472790-023FDF32-04A7-4CD5-B981-E2CFAD9E5753Q37250017-57A39F03-9A29-4719-8166-771E1CC5DAA3Q37856774-35CCDAEB-CE52-4521-BFB6-643143743D6FQ37969761-70C89B23-3A1E-4BA1-9634-C65A386902BBQ38223691-32A09DF6-3274-4FAA-BB8A-C8292BF91D5BQ39805609-8BECDD18-EB86-4425-AB04-38DFFA5564D2Q41960458-6F436F82-A4FD-4A74-86B8-1DF22DF7726EQ43104919-7ADC81BE-D625-4181-A5CC-E5D1DDD907C5Q43512154-AEE31B2E-BE4A-4803-BDE6-72C76715C35FQ43872486-D95FF5D5-DFB9-49C4-B5EB-B898DA84D0AEQ43947462-403E4FD7-F4EE-4AD9-B5A2-692081FBE1DFQ51657718-4019D9E0-32F8-4455-9087-BC8F6FEC1A6AQ51725890-507D1358-0327-4653-9732-7D354B5BB545Q51752899-328A6A5B-8745-4F51-9CDE-0EE25C9B77CFQ51915769-71038CCF-9E83-489D-8AF6-CE11E0664700Q51961147-24BC9C93-B23B-4DEA-9888-F349AA733A74Q58041737-85B6FDD7-F133-48C8-BC31-8E4A771EA24DQ58658653-70572BF9-9C4D-49A2-81E1-C7713DAE887D
P2860
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Is the molten globule a third phase of proteins?
@ast
Is the molten globule a third phase of proteins?
@en
Is the molten globule a third phase of proteins?
@nl
type
label
Is the molten globule a third phase of proteins?
@ast
Is the molten globule a third phase of proteins?
@en
Is the molten globule a third phase of proteins?
@nl
prefLabel
Is the molten globule a third phase of proteins?
@ast
Is the molten globule a third phase of proteins?
@en
Is the molten globule a third phase of proteins?
@nl
P2860
P356
P1476
Is the molten globule a third phase of proteins?
@en
P2093
D S Rokhsar
P2860
P304
P356
10.1073/PNAS.95.4.1490
P407
P577
1998-02-17T00:00:00Z