Conformational dependence on pH in tripeptides

Lala, Anil K. ; Anteunis, Marc J. O. ; Lala, Krishna (1976) Conformational dependence on pH in tripeptides Biochimica et Biophysica Acta (BBA) - Protein Structure, 453 (1). pp. 133-138. ISSN 0005-2795

Full text not available from this repository.

Official URL:

Related URL:


From the 1H-NMR study of Tyr-Gly-Gly and Phe-Gly-Gly in H2O and 2H2O as a function of pH it follows that these tripeptides display at least two and probably three conformational zones. Under slow exchange conditions of the peptidic NH-protons, coupling constants 3J(NH̲,CαH̲) may be extracted as the probe. At higher pH values shift values and 3J(α,β) of the side chain and the titration curves are indicative for these conformational alterations.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:31900
Deposited On:31 Mar 2011 06:25
Last Modified:31 Mar 2011 06:25

Repository Staff Only: item control page