Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
about
Protein knotting through concatenation significantly reduces folding stabilityExploring the folding energy landscape of a series of designed consensus tetratricopeptide repeat proteins.Repeat protein engineering: creating functional nanostructures/biomaterials from modular building blocks.Computational method allowing Hydrogen-Deuterium Exchange Mass Spectrometry at single amide Resolution.Structural and dynamic characterization of a freestanding acyl carrier protein involved in the biosynthesis of cyclic lipopeptide antibiotics.Mechanism of Protein Denaturation: Partial Unfolding of the P22 Coat Protein I-Domain by Urea Binding.Characterization of the unfolded state of repeat proteins.Ising Model Reprogramming of a Repeat Protein's Equilibrium Unfolding Pathway.Modulation of the multistate folding of designed TPR proteins through intrinsic and extrinsic factors.Non-random-coil behavior as a consequence of extensive PPII structure in the denatured state.Calorimetric study of a series of designed repeat proteins: modular structure and modular folding.Modulating repeat protein stability: the effect of individual helix stability on the collective behavior of the ensemble.Intermediates in the folding equilibrium of repeat proteins from the TPR family
P2860
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P2860
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh
2008年學術文章
@zh-hant
name
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
@en
type
label
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
@en
prefLabel
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
@en
P2860
P1476
Mapping the energy landscape of repeat proteins using NMR-detected hydrogen exchange
@en
P2093
Simon G J Mochrie
P2860
P304
P356
10.1016/J.JMB.2008.02.046
P407
P577
2008-02-29T00:00:00Z