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A 13 C spin‐lattice relaxation study of dipeptides containing glycine and proline: Mobility of the cyclic proline side chain
Author(s) -
Fossel E. T.,
Easwaran K. R. K.,
Blout E. R.
Publication year - 1975
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1975.360140504
Subject(s) - chemistry , proline , glycine , ring (chemistry) , cyclic peptide , stereochemistry , side chain , dipeptide , aqueous solution , relaxation (psychology) , carbon atom , crystallography , spin–lattice relaxation , amino acid , nuclear magnetic resonance , peptide , organic chemistry , polymer , social psychology , psychology , biochemistry , physics , nuclear quadrupole resonance
Molecular dynamics of the cyclic dipeptides cyclo (Gly‐ L ‐Pro), cyclo ‐(L‐Pro‐ L ‐Pro), and cyclo (L‐Pro‐D‐Pro) and the linear dipeptides L‐Pro‐Gly and cis and trans Gly‐ L ‐Pro were studied in neutral aqueous solution by 13 C nuclear magnetic resonance. Spinlattice relaxation times ( T 1 ) were determined for each individual carbon atom. The correlation times, τ, were derived from a semiquantitative analysis of the T 1 data. The correlation times of the proline ring carbons, β, γ, and δ suggest that the cyclic dipeptides have more restriction of conformational freedom in the proline ring than the linear dipeptides. This effect is most pronounced on the γ carbon.