A 13C Nuclear Magnetic Resonance Study of Histone H1 in 2-ChIoroethanol and Aqueous Solutions. Identification of Peaks Characteristic of Secondary Folding1
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/92/1/233/7555205/92-1-233.pdf
Cited by 17 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Conformation and dynamics of membrane proteins and biologically active peptides as studied by high-resolution solid-state 13C NMR;Journal of Molecular Structure;1998-01
2. 13C NMR Study on Conformation and Dynamics of the Transmembrane .alpha.-Helixes, Loops, and C-Terminus of [3-13C]Ala-Labeled Bacteriorhodopsin;Biochemistry;1994-12-01
3. A high-resolution solid-state 13C-NMR study on [1-13C]Ala and [3-13C]Ala and [1-13C]Leu and Val-labelled bacteriorhodopsin. Conformation and dynamics of transmembrane helices, loops and termini, and hydration-induced conformational change;European Journal of Biochemistry;1993-12
4. Conformation aspect of poly(.gamma.-oleyl L-glutamate) with long flexible side chains as studied by variable-temperature carbon-13 CP/MAS NMR spectroscopy;Macromolecules;1989-12
5. Conformation and dynamic aspects of poly(.gamma.-n-octadecyl L-glutamate) in the solid state and liquid-crystalline state as studied by variable-temperature carbon-13 CP/MAS NMR spectroscopy;Macromolecules;1988-01
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