Premium
Solution conformation of leiurotoxin I (scyllatoxin) by 1 H nuclear magnetic resonance
Author(s) -
Martins José C.,
Zhang Weiguo,
Tartar André,
Lazdunski Michel,
Borremans Frans A.M.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80115-y
Subject(s) - antiparallel (mathematics) , chemistry , proton , side chain , nuclear overhauser effect , deuterium , crystallography , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , physics , stereochemistry , nuclear physics , magnetic field , quantum mechanics , polymer
A proton NMR study at 500 MHz of leiurotoxin I in water is presented. Nearly complete sequence‐specific assignments of the individual backbone and side‐chain proton resonances were achieved using through‐bond and through‐space connectivities obtained from standard two‐dimensional NMR techniques. The secondary structure of this toxin is inferred from a combination of short‐range nuclear Overhauser enhancements, scalar couplings and proton/deuteron exchange rates. Three disulflde bridges locate the N‐terminal part (that is α‐helical from residue 6 to 16) on one side of a C‐terminal two stranded antiparallel β sheet (from Leu 18 to Val 29 ). The latter features a tight turn at Gly 23 ‐Asp 24 .