The backbone conformational entropy of protein folding: experimental measures from atomic force microscopy.
about
Loss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculationsConformational Entropy of Intrinsically Disordered Proteins from Amino Acid TriadsBioinspired laser-operated molecular locomotive.Sacrificial bonds and hidden length: unraveling molecular mesostructures in tough materials.Distributions in protein conformation space: implications for structure prediction and entropy.Effects of denaturants on the dynamics of loop formation in polypeptides.Toward an accurate theoretical framework for describing ensembles for proteins under strongly denaturing conditionsHuman topoisomerase I C-terminal domain fragment containing the active site tyrosine is a molten globule: implication for the formation of competent productive complex.Small-angle X-ray scattering of reduced ribonuclease A: effects of solution conditions and comparisons with a computational model of unfolded proteinsForce field bias in protein folding simulationsNanowires and nanostructures that grow like polymer molecules.Dentin on the nanoscale: Hierarchical organization, mechanical behavior and bioinspired engineering.Electrostatic and steric interactions determine bacteriorhodopsin single-molecule biomechanics.Context and force field dependence of the loss of protein backbone entropy upon folding using realistic denatured and native state ensemblesMultiscale Persistent Functions for Biomolecular Structure Characterization.The role of entropy in initializing the aggregation of peptides: a first principle study on oligopeptide oligomerization.Direct force measurement of single DNA-peptide interactions using atomic force microscopy.Elastic behavior of short compact polymers.Thermodynamics of Conformational Transitions in a Disordered Protein Backbone Model
P2860
Q28397040-6D37C735-82EF-480C-8532-FD5A0754AC8DQ28397659-C8986473-150E-404C-B109-B204861F2D8CQ31125030-6F427659-A08C-46B9-8D78-2504EB4495A1Q33228450-60F4EDFA-530F-4934-BC45-379F7CB22587Q34186180-CB85E14E-D89B-4F31-907A-5E5FA1CAE422Q34680372-B7619E16-E1BD-425B-B05B-9CF4D2AB7EA7Q34984722-646E052D-3023-46D3-ACF1-F38FCD95C9EEQ36012501-2003BCC9-962D-4D6E-B5F6-34E4797BB7D6Q37118723-70C2D8B3-5542-4F02-ADF8-EFEF5AFCB6F8Q37263580-516A2E0C-2CCB-448B-9EFE-FC7BE1353FAFQ38116493-FC3959F8-D962-4942-A4F1-970B84D845F2Q38729367-2620F23F-343E-44C4-9489-21BA00E0A936Q42183576-300DC25C-D68B-4365-841A-B5F5F598978DQ42207188-DE4AFD6A-D619-4155-9F2D-14A788421C4CQ47446522-423B04EA-E9C9-4AC4-B82E-A94F8DA3C6A9Q48786981-37429F86-19B8-429D-8F28-24EC70E6B964Q51063053-3BF80A46-92E6-41C2-8C69-C8F0328F6B44Q54311091-BE7E934A-1E07-4FA8-8718-BB5CF7FF1ECDQ57329080-F6016922-0F47-4055-93CE-A9AD81AF8FC3
P2860
The backbone conformational entropy of protein folding: experimental measures from atomic force microscopy.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh
2002年學術文章
@zh-hant
name
The backbone conformational en ...... from atomic force microscopy.
@en
The backbone conformational en ...... from atomic force microscopy.
@nl
type
label
The backbone conformational en ...... from atomic force microscopy.
@en
The backbone conformational en ...... from atomic force microscopy.
@nl
prefLabel
The backbone conformational en ...... from atomic force microscopy.
@en
The backbone conformational en ...... from atomic force microscopy.
@nl
P2093
P1476
The backbone conformational en ...... from atomic force microscopy.
@en
P2093
Helen G Hansma
James B Thompson
Kevin W Plaxco
Paul K Hansma
P304
P356
10.1016/S0022-2836(02)00801-X
P407
P577
2002-09-01T00:00:00Z