about
Energy landscape of a peptide consisting of alpha-helix, 3(10)-helix, beta-turn, beta-hairpin, and other disordered conformationsA backbone-based theory of protein foldingUV resonance Raman investigations of peptide and protein structure and dynamicsHow much of protein sequence space has been explored by life on Earth?The protein folding problemMultiple unfolding intermediates of human placental alkaline phosphatase in equilibrium urea denaturationProtein docking by the underestimation of free energy funnels in the space of encounter complexesA molecular interpretation of 2D IR protein folding experiments with Markov state modelsRobustness of atomistic Gō models in predicting native-like folding intermediates.Constraining local structure can speed up folding by promoting structural polarization of the folding pathwayEffects of frustration, confinement, and surface interactions on the dimerization of an off-lattice beta-barrel protein.Self-assembly of peptides into a beta-barrel motif.Posttransition state desolvation of the hydrophobic core of the src-SH3 protein domainProbing the folding free energy landscape of the Src-SH3 protein domain.Prediction of coordination number and relative solvent accessibility in proteins.A method to predict edge strands in beta-sheets from protein sequencesStylus: a system for evolutionary experimentation based on a protein/proteome model with non-arbitrary functional constraintsChSeq: A database of chameleon sequences.Influence of sequence changes and environment on intrinsically disordered proteins.Predicting Designability of Small Proteins from Graph Features of Contact MapsMembrane protein native state discrimination by implicit membrane models.Where soft matter meets living matter--protein structure, stability, and folding in the cell.Protein-protein alternative binding modes do not overlap.Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutionsTemperature-dependent downhill unfolding of ubiquitin. I. Nanosecond-to-millisecond resolved nonlinear infrared spectroscopy.Folding funnels, binding funnels, and protein functionFolding funnels and binding mechanisms.Protein folding pathways from replica exchange simulations and a kinetic network model.Folding and binding cascades: dynamic landscapes and population shifts.Structural and evolutionary relationships among protein tyrosine phosphatase domainsExtracting function from a beta-trefoil folding motifCharacterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experimentFunnel sculpting for in silico assembly of secondary structure elements of proteinsMolecular basis for the polymerization of octopus lens S-crystallinUnderstanding beta-hairpin formation by molecular dynamics simulations of unfolding.Model-based analysis of assembly kinetics for virus capsids or other spherical polymers.MC-PHS: a Monte Carlo implementation of the primary hydration shell for protein folding and design.Structured disorder and conformational selection.Secondary and tertiary structures of gaseous protein ions characterized by electron capture dissociation mass spectrometry and photofragment spectroscopy
P2860
Q22061727-B0761007-3AA1-4736-8EC9-9E9BCA1AA4FBQ24672727-57683356-F956-4655-8BAE-1AD15EAED35DQ26861612-7A9628E1-B7D3-40BE-BF3F-E7AEE636E782Q28277287-4CD26AA3-6818-4D21-A964-8A31D573AF5EQ28284812-9AC4386A-31F8-472F-9F62-C00A8F458B66Q28365189-AA265366-1EE4-4D30-9411-1CE721A8922EQ28473662-B570C5E2-9E7F-49DC-A621-37308D7FDE6AQ28660159-D3A70D00-8253-47DC-B613-AAC451244CDAQ30010022-99D99567-3878-4F7B-8F90-CABC21130427Q30155617-276DAEF3-2E14-4AE7-90DF-1B3B868544F8Q30159990-FAA867BE-EDE2-4BAF-919B-FCE693AB64E5Q30163926-69C86519-40D6-489C-99FC-0251CBF1B63FQ30164656-4D538568-06DC-4835-960E-DBA318AFE53DQ30165065-3C5CD89F-98AA-446F-8051-27EBB558AF24Q30330076-D7D42741-D056-44EE-B7EE-DB0CC42A2749Q30360862-A43A78DB-D33A-470D-BECD-CE6BB75F8C26Q30369737-6837E476-CCE7-4816-9FE9-51182810A1E4Q30374636-DFC9AAC0-03F8-4FD3-A1AF-5238B00F9788Q30380392-05257953-54A8-4DCF-9F38-3C341C21399CQ30387893-C855C294-C214-4EEF-AB23-343805AC423AQ30424545-5379BC09-A9CE-454A-95C3-E8F8CE5EE52CQ30428031-200CB24F-67E1-4281-A211-D4E97EF8C25CQ30432064-2C7B8A8D-617E-4BF8-9915-539934279BD6Q30499610-AD628DCC-73AA-4739-9437-049587578E5DQ31072074-8B7C27C5-8459-4CF7-ABA6-2C5DDDB19412Q33326719-DF2BB85F-2C02-43E9-A7C6-E693A74871B1Q33674287-14EFB36B-15E7-4053-9107-29B04A9B6BC7Q33743626-01DCCD09-BA97-4B42-88F9-DB7023010735Q33784400-4FA851D4-3F0A-4DDC-8FFA-195B19A1C2DAQ33876426-B7737C7F-EF50-4638-8C40-042A4DBE8B0DQ34012560-EB1A1ED8-DECF-4ECE-89A1-74EBBE5C3365Q34012949-AA615096-34C7-4613-A9D8-8E5EE149A39CQ34078456-385AAB70-914D-472E-92FD-044A543564E1Q34093249-61EEDE41-1356-4BC8-AEA0-550D8441471EQ34172883-D5E010CE-06D2-4E02-B4E9-3CC9691E1807Q34176707-676AB6F1-254F-4BDD-8791-523C05414CE8Q34178571-5BE87635-59AC-4887-99EC-FFB5450DC299Q34180313-358335EA-90ED-4CB4-8E73-E620148B977FQ34325473-7126D57D-9116-491E-9F8C-36EC0A215ABAQ34414608-4B27366D-C052-4EF3-BA0F-2AD2A22D27E0
P2860
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին 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
Polymer principles and protein folding
@ast
Polymer principles and protein folding
@en
Polymer principles and protein folding
@nl
type
label
Polymer principles and protein folding
@ast
Polymer principles and protein folding
@en
Polymer principles and protein folding
@nl
prefLabel
Polymer principles and protein folding
@ast
Polymer principles and protein folding
@en
Polymer principles and protein folding
@nl
P2860
P3181
P356
P1433
P1476
Polymer principles and protein folding
@en
P2093
P2860
P304
P3181
P356
10.1110/PS.8.6.1166
P407
P577
1999-06-01T00:00:00Z