High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.
about
The energetics of a three-state protein folding system probed by high-pressure relaxation dispersion NMR spectroscopy.Impact of hydrostatic pressure on an intrinsically disordered protein: a high-pressure NMR study of α-synucleinRole of cavities and hydration in the pressure unfolding of T4 lysozyme.The hydrophobic temperature dependence of amino acids directly calculated from protein structuresγS-crystallin proteins from the Antarctic nototheniid toothfish: a model system for investigating differential resistance to chemical and thermal denaturation.Amyloid transition of ubiquitin on silver nanoparticles produced by pulsed laser ablation in liquid as a function of stabilizer and single-point mutations."Invisible" conformers of an antifungal disulfide protein revealed by constrained cold and heat unfolding, CEST-NMR experiments, and molecular dynamics calculations.The Complex Energy Landscape of the Protein IscUCorrelated parameter fit of arrhenius model for thermal denaturation of proteins and cells.Computational investigation of cold denaturation in the Trp-cage miniprotein.Characterization of structure, dynamics, and detergent interactions of the anti-HIV chemokine variant 5P12-RANTES.Transition state and ground state properties of the helix-coil transition in peptides deduced from high-pressure studiesSimulated pressure denaturation thermodynamics of ubiquitin.A fully atomistic computer simulation study of cold denaturation of a β-hairpin.Study of protein folding under native conditions by rapidly switching the hydrostatic pressure inside an NMR sample cell.Consistent Treatment of Hydrophobicity in Protein Lattice Models Accounts for Cold DenaturationOn the mechanism of cold denaturation
P2860
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P2860
High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.
description
2013 nî lūn-bûn
@nan
2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@ast
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@en
type
label
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@ast
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@en
prefLabel
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@ast
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@en
P2093
P2860
P356
P1476
High-pressure NMR reveals clos ...... ein denaturation in ubiquitin.
@en
P2093
Lydia Nisius
Maciej Wiktor
Navratna Vajpai
P2860
P304
P356
10.1073/PNAS.1212222110
P407
P577
2013-01-02T00:00:00Z