about
Beyond the excluded volume effects: mechanistic complexity of the crowded milieuCold-induced changes in the protein ubiquitinA method for solution NMR structural studies of large integral membrane proteins: reverse micelle encapsulation.Measurement and control of pH in the aqueous interior of reverse micelles.NMR-based structural biology of proteins in supercooled water.Reverse micelles as a tool for probing solvent modulation of protein dynamics: Reverse micelle encapsulated hemoglobin.The non-uniform early structural response of globular proteins to cold denaturing conditions: a case study with Yfh1.Signatures of protein thermal denaturation and local hydrophobicity in domain specific hydration behavior: a comparative molecular dynamics study.Optimization of NMR spectroscopy of encapsulated proteins dissolved in low viscosity fluids.Mapping the hydration dynamics of ubiquitinHighly anomalous energetics of protein cold denaturation linked to folding-unfolding kineticsHigh-resolution NMR spectroscopy of encapsulated proteins dissolved in low-viscosity fluidsThe Complex Energy Landscape of the Protein IscUProtein folding and unfolding studied at atomic resolution by fast two-dimensional NMR spectroscopyOptimized reverse micelle surfactant system for high-resolution NMR spectroscopy of encapsulated proteins and nucleic acids dissolved in low viscosity fluidsReverse micelle encapsulation of membrane-anchored proteins for solution NMR studiesObservation of solvent penetration during cold denaturation of E. coli phosphofructokinase-2.Simulations of the confinement of ubiquitin in self-assembled reverse micelles.An alpha-helical peptide in AOT micelles prefers to be localized at the water/headgroup interface.The cold denatured state of the C-terminal domain of protein L9 is compact and contains both native and non-native structureMutational analysis of m-values as a strategy to identify cold-resistant substructures of the protein ensemble.Structural and mechanical properties of glassy water in nanoscale confinement.
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
name
Cold denaturation of encapsulated ubiquitin.
@ast
Cold denaturation of encapsulated ubiquitin.
@en
type
label
Cold denaturation of encapsulated ubiquitin.
@ast
Cold denaturation of encapsulated ubiquitin.
@en
prefLabel
Cold denaturation of encapsulated ubiquitin.
@ast
Cold denaturation of encapsulated ubiquitin.
@en
P2093
P2860
P356
P1476
Cold denaturation of encapsulated ubiquitin.
@en
P2093
A Joshua Wand
Charles R Babu
Maxim S Pometun
Ronald W Peterson
P2860
P304
10652-10653
P356
10.1021/JA0628654
P407
P577
2006-08-01T00:00:00Z