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15 N nmr spectroscopy. I. Polysarcosine and related sequence polypeptides
Author(s) -
Kricheldorf Hans R.,
Hull William E.,
Formacek Viktor
Publication year - 1977
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.1977.360160802
Subject(s) - chemistry , isomerization , nuclear magnetic resonance spectroscopy , peptide , peptide bond , nitrogen atom , sequence (biology) , residue (chemistry) , crystallography , spectroscopy , stereochemistry , chemical shift , spectral line , relaxation (psychology) , nmr spectra database , nuclear overhauser effect , peptide sequence , two dimensional nuclear magnetic resonance spectroscopy , organic chemistry , catalysis , physics , biochemistry , social psychology , psychology , quantum mechanics , astronomy , group (periodic table) , gene
The natural abundance 15 N nmr spectra of linear polysarcosine ( DP = 35) has been recorded in Me 2 SO and H 2 O solution. Because of cis / trans isomerization at the peptide bond, a broad signal with several splittings was observed. These splittings appear to reflect the influence of three peptide bonds on a single N atom. The 15 N signals from the sequence polypeptides (β‐Ala‐Sar‐Gly) n and (β‐Ala‐Sar‐ D , L ‐Ala) n also show a cis / trans splitting, as well as chemical shifts which are dependent on the peptide sequence. The tertiary nitrogen of the sarcosyl residue has a T 1 relaxation time which is longer than the T 1 for secondary nitrogens of the other amino acids. The nuclear Overhauser effect is also discussed.