## Abstract The possible influence of thermal motion on ^1^H chemical shifts is discussed for a small stable protein, the bovine pancreatic Kunitz trypsin inhibitor (BPTI). The thermal effects on the aromatic side chains and on the backbone are treated separately. The thermal motion of the aromatic
β¦ LIBER β¦
Sidechain Torsional Potentials and Motion of Amino Acids in Proteins: Bovine Pancreatic Trypsin Inhibitor
β Scribed by Bruce R. Gelin and Martin Karplus
- Book ID
- 123653213
- Publisher
- National Academy of Sciences
- Year
- 1975
- Tongue
- English
- Weight
- 918 KB
- Volume
- 72
- Category
- Article
- ISSN
- 0027-8424
- DOI
- 10.2307/64632
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