The Role of Trp in Arg-Rich Paddle Domain-Lipid Interaction
✍ Scribed by Ye, Weihua; Unnersåle, Sofia; Mäler, Lena
- Book ID
- 122969409
- Publisher
- Biophysical Society
- Year
- 2014
- Tongue
- English
- Weight
- 41 KB
- Volume
- 106
- Category
- Article
- ISSN
- 0006-3495
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Complexes formed between dimyristoylphosphatidylcholine (DMPC) and the peptide pentagastrin or [Arg4]pentagastrin were examined by 31P- and 2H-NMR. The cationic [Arg4]pentagastrin produces larger changes in the lipid NMR spectra than does the anionic pentagastrin. 31P-NMR spectra of DMPC with [Arg4]
## Abstract Human pancreatic lipase (HPL) consists of two functional domains: an N‐terminal catalytic domain (N‐HPL), and a β‐sandwich C‐terminal domain (C‐HPL) involved in the binding process between HPL and colipase. Structural similarities between C‐HPL and C2 domains have suggested another func