A Pulsed-Field Gradient NMR Study of Bovine Pancreatic Trypsin Inhibitor Self-Association †
✍ Scribed by Ilyina, Elena; Roongta, Vikram; Pan, Hong; Woodward, Clare; Mayo, Kevin H.
- Book ID
- 126083052
- Publisher
- American Chemical Society
- Year
- 1997
- Tongue
- English
- Weight
- 142 KB
- Volume
- 36
- Category
- Article
- ISSN
- 0006-2960
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The kinetics of the formation of the complex between bovine P-trypsin and the porcine pancreatic secretory trypsin inhibitor (PSTI; Kaza-type inhibitor) was investigated following the spectral changes associated with the displacement of proflavine from the enzyme, upon inhibitor binding, between pH
## Abstract Pulsed‐field gradient (PFG) NMR spectroscopy was used to characterize the interactions between a series of small peptides and sodium dodecyl sulfate (SDS) micelles. The study was undertaken because peptide–micelle interactions are often exploited in the chromatographic analysis of compl