1H nuclear magnetic resonance studies of the interaction of urea with hen lysozyme. Origins of the conformational change induced in hen lysozyme by N-acetylglucosamine oligosaccharides.
about
Roles of dimerization in folding and stability of ketosteroid isomerase from Pseudomonas putida biotype BFragment-based identification of determinants of conformational and spectroscopic change at the ricin active siteWater and urea interactions with the native and unfolded forms of a beta-barrel protein.Effects of organic solvents on protein structures: observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide.Time-dependent X-ray diffraction studies on urea/hen egg white lysozyme complexes reveal structural changes that indicate onset of denaturationAnion binding to the ubiquitin molecule.
P2860
1H nuclear magnetic resonance studies of the interaction of urea with hen lysozyme. Origins of the conformational change induced in hen lysozyme by N-acetylglucosamine oligosaccharides.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
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1992年學術文章
@zh-hant
name
1H nuclear magnetic resonance ...... lglucosamine oligosaccharides.
@en
type
label
1H nuclear magnetic resonance ...... lglucosamine oligosaccharides.
@en
prefLabel
1H nuclear magnetic resonance ...... lglucosamine oligosaccharides.
@en
P1476
1H nuclear magnetic resonance ...... lglucosamine oligosaccharides.
@en
P2093
P356
10.1016/0022-2836(92)90677-C
P407
P50
P577
1992-09-01T00:00:00Z