
TY  - JOUR
A1  - Beilharz, GB 
A1  - Fong, J 
A1  - Mack, POL 
A1  - Robertson, AV 
A1  - Wright, PE 
T1  - A proton N.M.R. study of the conformation of Trp-Gly-Ala-Glu in dimethyl sulfoxide and water
JF  - Australian Journal of Chemistry
JO  - Aust. J. Chem.
Y1  - 1983
VL  - 36
IS  - 4
SP  - 751
EP  - 758
KW  - 
UR  - https://doi.org/10.1071/CH9830751 
N2  - Proton nuclear magnetic resonance parameters are reported for Trp-Gly-Ala-Glu, constituting residues 115-118 of bovine myelin basic protein, in dimethyl sulfoxide solution. The 3JNH,&#945; vicinal coupling constants which were used to determine &#934; torsional angles, together with the amide proton temperature coefficients, are consistent with a type I ,&#946;turn conformation. Amide proton tempera- ture coefficients obtained for the peptide dissolved in H2O at pH 1.3, 4.6 and 6.5 indicate that the peptide does not adopt any highly preferred folded conformation in water. These findings lend support to previous reports of a reverse turn involving the Trp-Gly-Ala-Glu portion of the encephalitogenic nonapeptide Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Lys from bovine myelin basic protein. 
ER  -

