Open Access1 H‐NMR assignment and secondary structure of a Herpes simplex virus glycoprotein D‐1 antigenic domain
Author(s) -
WILLIAMSON Michael P.,
HALL Michael J.,
HANDA Balraj K.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09786.x
Subject(s) - protein secondary structure , chemistry , amide , herpes simplex virus , peptide , nuclear overhauser effect , stereochemistry , nuclear magnetic resonance spectroscopy , random coil , virus , virology , biochemistry , biology
The peptide αAhx‐Met‐Ala‐Asp‐Pro‐Asn‐Arg‐Phe‐Arg‐Gly‐Lys‐Asp‐Leu‐Pro‐Val‐Leu‐Asp‐Gln‐ Leu‐Thr‐Asp‐Pro‐Pro‐αAhx (ɛAhx = 6‐aminohexanoyl), the antigenic sequence 11–32 from Herpes simplex virus glycoprotein D‐1, has been synthesised. Its 1 H‐NMR spectrum has been assigned by a combination of two‐dimensional techniques in H 2 O and 2 H 2 O. Its secondary structure has been defined by nuclear Overhauser effects and amide proton exchange rates, and also to some extent chemical shifts, coupling constants and amide proton temperature coefficients. These latter parameters are shown to be less reliable as guides to secondary structure. The peptide has a helical (type I/III) turn at residues Pro‐14—Asn‐15 and helical structure at residues Lys‐20–Val‐24, in rapid equilibrium with random‐coil structure. A β‐turn at residues Arg‐18—Gly‐19 may be present as a minor component. These locations of secondary structure correspond with previously determined regions of antigenic activity.