Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles.
about
Snapshots of a protein folding intermediateOrigin of the conformational heterogeneity of cardiolipin-bound cytochrome C.Conformational properties of cardiolipin-bound cytochrome cHow EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosomeKinetic consequences of native state optimization of surface-exposed electrostatic interactions in the Fyn SH3 domain.Learning To Fold Proteins Using Energy Landscape Theory.Multiscale enhanced sampling of intrinsically disordered protein conformations.Electrostatics, structure prediction, and the energy landscapes for protein folding and binding.Chemical frustration in the protein folding landscape: grand canonical ensemble simulations of cytochrome c.Modulating native-like residual structure in the fully denatured state of photoactive yellow protein affects its refolding.Multi-scaled explorations of binding-induced folding of intrinsically disordered protein inhibitor IA3 to its target enzyme.Denatured states of low-complexity polypeptide sequences differ dramatically from those of foldable sequencesThe origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein foldingFrom the Cover: Charge interactions can dominate the dimensions of intrinsically disordered proteins.The folding energy landscape and free energy excitations of cytochrome cImportance of electrostatic interactions in the association of intrinsically disordered histone chaperone Chz1 and histone H2A.Z-H2B.Mechanisms of cellular proteostasis: insights from single-molecule approachesModulation of folding energy landscape by charge-charge interactions: linking experiments with computational modelingRegulation and aggregation of intrinsically disordered peptidesTopology, structures, and energy landscapes of human chromosomes.Folding without charges.Nonnative interactions regulate folding and switching of myristoylated protein.Quantifying the topography of the intrinsic energy landscape of flexible biomolecular recognitionSingle-molecule spectroscopy of the temperature-induced collapse of unfolded proteins.Reduced model captures Mg(2+)-RNA interaction free energy of riboswitchesGenomic Energy Landscapes.Cytochrome unfolding pathways from computational analysis of crystal structures.The ribosome modulates nascent protein folding.Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling.Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Opposing Intermolecular Tuning of Ca2+ Affinity for Calmodulin by Neurogranin and CaMKII Peptides.Mimicking Tyrosine Phosphorylation in Human Cytochrome c by the Evolved tRNA Synthetase Technique.Cytochrome c: A Multifunctional Protein Combining Conformational Rigidity with Flexibility
P2860
Q27675899-BFEC7A8B-9307-471F-AC22-C767A6538BB4Q28391414-CC6FDFC0-1668-4BE7-89AA-C33706D0EE67Q28395379-F9246DF4-19E3-40AA-846E-3219315723F9Q28822195-21637312-8551-45C3-9F6B-1460AA6A9FE9Q30010189-B991F141-281E-4DC1-BA72-EACCD5BFC48FQ30367734-FB02A108-39F7-46DE-8CF4-3BCA39894B35Q30375439-4C9F5EAC-B519-4D16-BC87-65829CF2E4E2Q30376811-AD94CA49-8FA2-488C-9417-00AF3345D27BQ33740575-A7DDFCF4-C7F2-418B-A539-B5AC9499C676Q33800083-610F7AB6-88F6-4B8E-841B-BDEA68B7345CQ33872107-A4380D9C-8C86-4680-A670-10A2BC2BD080Q33953210-4FDE4410-8227-46FF-B839-44CA98045001Q33999576-E8AA979E-4073-4C7A-A909-07E9DAABDB18Q34093140-1FFD6923-763D-43E7-AEB7-198152EBFFF2Q34094030-1A1A3BB0-B716-4046-AF18-69FF9402997AQ34341336-027AEA8C-E354-4662-8BB0-CDEA60E2CDCCQ34422820-E20FB0C8-25C9-4763-A66C-4DF9B6339769Q35031498-E811DCB5-BF18-4931-AA68-4FCF38ACB6A3Q35157010-87AB08DA-F032-4AB9-A05B-184100D098EBQ35616170-1D72FACC-B906-4C36-A292-F40E0D28BBEDQ35889494-87D3B577-0FC8-4B95-B5F8-B454EFF7556DQ36397857-1DEDA3CA-AE17-4509-8E25-6534728C4240Q36967812-EEC7DB7B-5766-41EB-8D09-06949BE6D285Q37469603-BC32B5DE-7FE8-410C-8A60-B55CFF14F00DQ37686070-E48973F2-CAF8-4273-B5A3-E3FACFAAEE02Q38969583-44E6F464-615A-4D67-B523-C830418EB5C8Q40276181-80FA015A-FC08-440B-88CE-39C7AFB248B3Q42714513-EA588F27-9605-4208-A2A7-6EE106780E78Q47119009-F982A2C1-D7DC-47B3-9BC1-64E88FDCB532Q47214435-38E67FAF-3239-48AF-938B-677BAD05F06AQ51081890-3972527A-0167-4976-9C97-19C1CE24C4B4Q52862738-04639DDF-7DDB-4B54-B08D-64B19B862DC2Q59072658-CBF29A23-C505-45F1-8060-0E6C4D67A354
P2860
Electrostatic effects on funneled landscapes and structural diversity in denatured protein ensembles.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 30 January 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Electrostatic effects on funne ...... n denatured protein ensembles.
@en
Electrostatic effects on funne ...... n denatured protein ensembles.
@nl
type
label
Electrostatic effects on funne ...... n denatured protein ensembles.
@en
Electrostatic effects on funne ...... n denatured protein ensembles.
@nl
prefLabel
Electrostatic effects on funne ...... n denatured protein ensembles.
@en
Electrostatic effects on funne ...... n denatured protein ensembles.
@nl
P2093
P2860
P356
P1476
Electrostatic effects on funne ...... n denatured protein ensembles.
@en
P2093
Ekaterina V Pletneva
Jay R Winkler
Patrick Weinkam
P2860
P304
P356
10.1073/PNAS.0813120106
P407
P577
2009-01-30T00:00:00Z