about
Spinocerebellar ataxia-13 Kv3.3 potassium channels: arginine-to-histidine mutations affect both functional and protein expression on the cell surfaceSite-specific infrared probes of proteinsThe effect of chemical chaperones on the assembly and stability of HIV-1 capsid proteinRestoration of structural stability and ligand binding after removal of the conserved disulfide bond in tear lipocalin.Cosolvent and crowding effects on the polymerization kinetics of actin.How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)Experimental validation of the role of trifluoroethanol as a nanocrowder.When does trimethylamine N-oxide fold a polymer chain and urea unfold it?Forced folding of a disordered protein accesses an alternative folding landscape.Synergy in protein-osmolyte mixtures.Regulation and aggregation of intrinsically disordered peptidesBiomolecular Crowding Arising from Small Molecules, Molecular Constraints, Surface Packing, and Nano-Confinement.Solute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding abilityMolecular mechanism for the preferential exclusion of TMAO from protein surfaces.Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.Aggregation of Chameleon Peptides: Implications of α-Helicity in Fibril FormationDistinctive solvation patterns make renal osmolytes diverse.Reaching new levels of realism in modeling biological macromolecules in cellular environments.Cosolutes, Crowding, and Protein Folding Kinetics.Trimethylamine-N-Oxide Treatment Induces Changes in the ATP-Binding Cassette Transporter A1 and Scavenger Receptor A1 in Murine Macrophage J774A.1 cells.Effects of salt or cosolvent addition on solubility of a hydrophobic solute in water: Relevance to those on thermal stability of a protein.Trimethylamine-N-oxide: its hydration structure, surface activity, and biological function, viewed by vibrational spectroscopy and molecular dynamics simulations.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Trimethylamine-N-oxide switches from stabilizing nature: A mechanistic outlook through experimental techniques and molecular dynamics simulation.Combined pressure and cosolvent effects on enzyme activity - a high-pressure stopped-flow kinetic study on α-chymotrypsin.Are stabilizing osmolytes preferentially excluded from the protein surface? FTIR and MD studies.Chaperones rescue the energetic landscape of mutant CFTR at single molecule and in cell.Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine.Protonation of trimethylamine N-oxide (TMAO) is required for stabilization of RNA tertiary structure.Interactions of S-peptide analogue in aqueous urea and trimethylamine-N-oxide solutions: a molecular dynamics simulation study.Conformational Ensembles of α-Synuclein Derived Peptide with Different Osmolytes from Temperature Replica Exchange Sampling.Using a FRET Library with Multiple Probe Pairs To Drive Monte Carlo Simulations of α-Synuclein.TMAO mediates effective attraction between lipid membranes by partitioning unevenly between bulk and lipid domains.Crowders and Cosolvents-Major Contributors to the Cellular Milieu and Efficient Means to Counteract Environmental Stresses.Can an ammonium-based room temperature ionic liquid counteract the urea-induced denaturation of a small peptide?Modulation of the Polymerization Kinetics of α/β-Tubulin by Osmolytes and Macromolecular Crowding.Effects of Trimethylamine-N-oxide on the Conformation of Peptides and its Implications for Proteins.
P2860
Q24294515-B5D38D64-F2E3-408C-8F55-809BB06C0A3EQ26866007-E4AE4F85-BF2F-4017-8F11-A607650E0CDCQ28486018-4F8ADA89-1CDA-41E8-9EF0-54F4962FB314Q30366816-E59897A2-0198-4AC6-A545-9EBE06E52489Q30368437-B586909F-479F-4B08-8D6E-C100D32F1980Q30376640-FA0E5463-3175-49B2-82B7-C06D3C4B0082Q30419579-55CAAD2C-F2FF-4EA0-9C5E-503C6FE04685Q30830001-287F0F64-65D2-45E8-A02A-1078E7F81FA3Q34281435-2EB9D9EA-169C-4993-8F52-688F7F167D75Q34380720-C4F5BA38-3270-48D7-9944-A8318905C357Q34856957-AAB0144E-AAC8-4E30-9489-9B97D10B890DQ34917876-4042D436-ADB1-49AA-9842-DE7FB32EF7DAQ35157010-634F3D07-17A3-40DC-8732-04758D94A6A3Q36176612-8EE19544-997B-414E-A0B3-04CDC62A2FA9Q36331161-95F00AE7-08CB-4AF2-92E2-0A631216181DQ36501094-9F4F64B9-685B-4FDD-8BFA-904CA5143858Q37013963-BB509645-1581-4C24-ACBF-D7B87A41DBD3Q37075230-C9478F97-6E81-4D6B-835A-F83C62742364Q37299335-BBED9104-747E-4E75-B344-DEC94C605503Q38137656-8113B42E-5861-4069-ABE2-D0EB291DDCE1Q38730102-DE37A7B9-DD3B-40C4-8D8D-FFD24A2F8498Q38832001-47212157-AEC9-435D-BED3-71B619061622Q38971588-51DC6DE7-806B-4CB9-8AC6-44DED0323453Q39114648-8EBAED2A-2D21-4F51-A1CE-B3D1E0160733Q39223628-1C3524D0-546A-4101-A1D5-5A8A8E6B870AQ39647606-0369440A-1066-43A6-B90B-0847F553E33FQ40630355-E940B17D-0422-419E-88F7-524310A600F1Q40637758-6C9FCA5A-895A-434F-8008-E1231EBAAB56Q41565850-E27F37EE-52A4-481F-A58C-0E7E0FB1B0F0Q41600734-BE050169-79DB-40E1-B2F9-F3F1A4B9E274Q42017214-654341A4-0F34-4502-A429-AA1B38644FC3Q42863627-2CBDFC49-BF2B-4FFA-ACA8-28017F250D9CQ43713287-ABABADBB-48BC-4EB1-B0FB-CDBA24572441Q47119009-9260141F-00B8-437F-BA1C-39E8A95BACEAQ47213644-B787E9E9-8664-4130-A5A5-FFA71E77B377Q47433206-8ABF9FCD-02DD-43EA-BF09-6BC0010734B7Q47792971-3DEA9358-2FAC-4606-8884-EE281EC9B706Q48161856-F628F03D-6412-4114-913B-5953D18BA373Q48245522-2CDA6C47-25AC-4C47-8320-9FE61430455CQ49831251-2D3CBBA2-99D7-45EC-A961-48BAF54F7630
P2860
description
2011 nî lūn-bûn
@nan
2011 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Entropic stabilization of proteins by TMAO
@ast
Entropic stabilization of proteins by TMAO
@en
type
label
Entropic stabilization of proteins by TMAO
@ast
Entropic stabilization of proteins by TMAO
@en
prefLabel
Entropic stabilization of proteins by TMAO
@ast
Entropic stabilization of proteins by TMAO
@en
P2093
P2860
P3181
P356
P1476
Entropic stabilization of proteins by TMAO
@en
P2093
D Thirumalai
Govardhan Reddy
John E Straub
Samuel S Cho
P2860
P304
P3181
P356
10.1021/JP207289B
P407
P577
2011-11-17T00:00:00Z