Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.
about
Structural characterization of a mutant peptide derived from ubiquitin: Implications for protein foldingMolecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics.The effects of organic solvents on the folding pathway and associated thermodynamics of proteins: a microscopic view.Principles of protein folding--a perspective from simple exact models.Water plays an important role in osmolyte-induced hairpin structure change: a molecular dynamics simulation study.Effects of Fe(II)/H2O2 oxidation on ubiquitin conformers measured by ion mobility-mass spectrometry.Conformational changes during the nanosecond-to-millisecond unfolding of ubiquitin.Phage viability in organic media: insights into phage stability.Effects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide.Temperature-dependent downhill unfolding of ubiquitin. I. Nanosecond-to-millisecond resolved nonlinear infrared spectroscopy.The hydrogen exchange core and protein folding.NMR studies on thermal stability of α-helix conformation of melittin in pure ethanol and ethanol-water mixture solvents.High-resolution, high-pressure NMR studies of proteins.Effects of select anions from the Hofmeister series on the gas-phase conformations of protein ions measured with traveling-wave ion mobility spectrometry/mass spectrometry.Probing the folding transition state of ubiquitin mutants by temperature-jump-induced downhill unfolding.Protein folding dynamics: the diffusion-collision model and experimental data.Hexafluoroacetone hydrate as a structure modifier in proteins: characterization of a molten globule state of hen egg-white lysozyme.Transfer of structural elements from compact to extended states in unsolvated ubiquitinA model of the molten globule state from molecular dynamics simulations.On the origin of the enthalpy and entropy convergence temperatures in protein foldingEvidence for two new solution states of ubiquitin by IMS-MS analysis.Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR.Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.Anion binding to the ubiquitin molecule.Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation.Autonomous folding of a peptide corresponding to the N-terminal beta-hairpin from ubiquitinSolution dependence of the collisional activation of ubiquitin [M + 7H](7+) ions.Characterization of a partially structured state in an all-beta-sheet protein.Secondary-structure analysis of alcohol-denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy.Equilibrium NMR studies of unfolded and partially folded proteins.Protein intrinsic disorder negatively associates with gene age in different eukaryotic lineages.Unfolding dynamics of the protein ubiquitin: insight from simulation.Identification and ab initio simulations of early folding units in proteins.Temperature-dependent downhill unfolding of ubiquitin. II. Modeling the free energy surface.Unified perspective on proteins: a physics approach.Mimicking lipid-binding-induced conformational changes in the human apolipoprotein E N-terminal receptor binding domain effects of low pH and propanol.
P2860
Q27629222-308EF71B-2A42-4FB7-A4F1-541DBE87CAA0Q30361948-E581B23A-3663-4167-B4FE-8B7529BB67B7Q30383589-7166A2DD-96CB-4D22-BA60-997D61E9E98CQ30417429-41BE9A63-51E1-4898-8210-F4974D644B13Q30422298-DE2E92FA-52D6-4DCF-9D30-EDDA4751CED7Q30424397-AEC38C69-13C0-4982-B048-B643BD2A6C60Q30499610-A919B8B1-584C-4631-A997-DB4BF62AB689Q30654727-1B00CDF3-2444-4267-8A24-785492207C90Q32167485-43C6C3D5-1F80-4AFA-859D-643901464B3FQ33326719-19B7BB97-1F83-46CD-AAED-31DECE24D463Q33714720-1F6813D6-B6A7-4FCC-83D1-4451A3FE7FA0Q34034601-76E7BE5A-D0FA-4129-B426-21BAE5413351Q34168473-8276591C-F059-46C9-8AE5-1057454E97E8Q35538523-5245363D-8372-4F46-87BC-537CE6CB4974Q35870253-46B0E3D1-0651-40B2-A353-51EA01C6721FQ36278710-C393BD23-6023-4F23-B9BF-AF4E7C491490Q36280361-686C5BAE-8B46-4E53-B19B-0CAE70CF5C7DQ36828634-36B68DF3-2843-484C-9A9D-B2FE6946AD22Q37045931-7D03E321-001A-4A71-A5E0-1757796249A0Q37233653-5A61FA73-A56C-4A93-9B65-BE762C1B8533Q38706259-D3783891-EDA0-47E0-845E-4B17E7358004Q39824027-14BD3671-C12F-4FF0-AB4A-E94E317384A8Q41894906-71C6FB62-9EC6-4C2C-9A65-44D91B2AC555Q42776286-6C44949D-E69D-4A64-BFAF-11C989728927Q42842821-59D236BF-795C-4DCE-B71C-46C4A4941F86Q42847121-863B3450-894C-4491-B21B-62D5E9C001E5Q42909554-1468786B-9661-4874-BC3C-87CCD177DB02Q42985273-92380B9B-2BA3-4240-BCDA-6BC50FF67EE1Q44245143-F672FACA-645D-4D7F-B3CC-543DB32FEADAQ46162800-4FE8715A-5BA7-4666-ABAB-C6C6FFF6922BQ46324799-38A38629-BBEC-4719-BB56-701ABED5897DQ46871971-313BAFCB-92F7-453A-BC09-CC5648BB25F7Q52070055-C4CCA6C4-DD6A-4D7F-9694-D04FD6163077Q52586107-1385D8C5-427E-410D-BADE-52C130A515FBQ53629521-4055FF0E-A289-448F-BCDD-78847B48762EQ54078676-ECDA005B-0BDE-4E8F-8F7F-04D2433F5955
P2860
Characterization of a partially denatured state of a protein by two-dimensional NMR: reduction of the hydrophobic interactions in ubiquitin.
description
1991 nî lūn-bûn
@nan
1991 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի մարտին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
name
Characterization of a partiall ...... bic interactions in ubiquitin.
@ast
Characterization of a partiall ...... bic interactions in ubiquitin.
@en
type
label
Characterization of a partiall ...... bic interactions in ubiquitin.
@ast
Characterization of a partiall ...... bic interactions in ubiquitin.
@en
prefLabel
Characterization of a partiall ...... bic interactions in ubiquitin.
@ast
Characterization of a partiall ...... bic interactions in ubiquitin.
@en
P2093
P356
P1433
P1476
Characterization of a partiall ...... bic interactions in ubiquitin.
@en
P2093
Harding MM
Williams DH
Woolfson DN
P304
P356
10.1021/BI00226A020
P407
P577
1991-03-01T00:00:00Z