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
✍ Scribed by Satoru TUZI; Akira NAITO; Hazime SAITÔ
- Book ID
- 115130410
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 729 KB
- Volume
- 218
- Category
- Article
- ISSN
- 1432-1327
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## Abstract We have so far demonstrated that well‐resolved and site‐specifically assigned ^13^C peaks as recorded by site‐directed NMR study on ^13^C‐labeled membrane proteins can serve as a convenient probe to reveal their local conformation and dynamics. We attempted here to clarify the extent to
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