File(s) under permanent embargo
Solution structure of pardaxin P-2
journal contribution
posted on 1991-01-01, 00:00 authored by M G Zagorski, D G Norman, Colin BarrowColin Barrow, T Iwashita, K Tachibana, D J PatelPardaxin is a mucosal secretion of the Pacific sole Pardachirus pavoninus that exhibits unusual shark repellent and surfactant properties [Thompson, S. A., Tachibana, K., Nakanishi, K., & Kubota, I. (1986) Science 233, 341-343]. This 33 amino acid polypeptide folds into ordered structures in trifluoroethanol-water solution and in micelles but adopts a random-coiled structure in water solution. The complete proton NMR spectrum of pardaxin P-2 has been assigned in CF 3 CD 2 OD/H 2 O (1:1) solution, and the three-dimensional structure has been elucidated with distance restrained molecular dynamics calculations. It is demonstrated that peptide segments within the 7-11 and 14-26 residue stretches are helical while residues at the C- and N-terminus exist predominantly in extended conformations in solution. The dipeptide 12-13 segment connecting the two helices exists as a bend or a hinge allowing the two helices to be oriented in a L-shaped configuration. These studies establish that pardaxin P-2 adopts a novel amphiphilic helix (7-11)-bend (12-13)-helix (14-26) motif with Pro-13 forming the focal point of the turn or bend between the two helices.
History
Journal
BiochemistryVolume
30Issue
32Pagination
8009 - 8017Publisher
American Chemical SocietyLocation
Washington, D.C.Publisher DOI
ISSN
0006-2960eISSN
1520-4995Language
engPublication classification
C1.1 Refereed article in a scholarly journalCopyright notice
1991, American Chemical SocietyUsage metrics
Categories
No categories selectedLicence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC