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

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/000527...

Related URL: http://dx.doi.org/10.1016/0005-2795(76)90257-9

Abstract

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.

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