NDLI: Analysis Of Short Interproton Distances In Proline Peptides As A Guide In The Interpretation Of Nuclear Overhauser Effects

Content Provider	Indian Institute of Science (IISc)
Author	Ramakrishnan, Chandrashekharan Sowdhamini, Ramanathan Balaram, Padmanabhan
Copyright Year	1988
Abstract	The conformational dependence of interproton distances in model proline peptides has been investigated in order to facilitate interpretation of the results of Nuclear Overhauser Effect (NOE) studies on such peptides. For this purpose two model systems, namely, Ac-Pro-NHMe and Ac-Pro-X-NHMe have been chosen and used. In the former, short interproton distances detectable in NOE experiments permit a clear distinction between conformations with Pro (S\|(B = -300 (helical region) and those in which (S\|(B is around 1200 (polyproline region). For the latter, the variation of distances between the protons of methyl amide and the Pro ring have been studied by superimposing on the Ramachandran map in the ((Sz(B3, (S\|(B3) plane. The results show that (Sb(B-turns and non-(Sb(B-turn conformations can be readily distinguished from NOE data and such long range NOEs should be detectable for specific non-(Sb(B-turn conformations. NOEs involving C(Sb(B and C(Sd(B protons are particularly sensitive to the state of pyrrolidine ring puckering.
File Format	PDF
Journal	PeerReviewed
Language	English
Publisher	UOCHB
Publisher Date	1988-11-01
Access Restriction	Authorized
Subject Keyword	Molecular Biophysics Unit
Content Type	Text
Resource Type	Article

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