151545-28-7Relevant articles and documents
13C-N.M.R.-SPECTRAL STUDY OF THE MODE OF BINDING OF Gd(3+) TO VARIOUS GLUCOPEPTIDES
Dill, Kilian,Daman, Marsha E.,Batstone-Cunningham, Ron L.,Lacombe, Jean M.,Pavia, Andre A.
, p. 123 - 136 (1983)
Natural-abundance, 13C-n.m.r. spectroscopy was used to study the mode of binding of Gd(3+) to mono-O-glycosylated L-serine and tripeptides variously composed of Gly and L-Thr.When the amino and carboxyl groups of the amino acid are not blocked, strong interaction of Gd(3+) with them is observed; this is also readily apparent with some related, nonglycosylated peptides.When the amino and carboxyl and carboxyl groups of the amino acid are blocked, noticeble interaction of Gd(3+) with the glycosidic oxygen atom (O-3) and O-2' for the glycopeptide containing α-D-Galp, and with O-3 and N-2' for the glycopeptide containing α-D-GalpNAc, is observed.Weak interactions are also possible with O-4' and O-6' of the glycosyl groups.Although the amino acids were protected, these metal ion-carbohydrate interactions may still be mediated, to some extent, by the acetyl protecting the amino group and by the ester group on the amino acid.
Partial Molar Heat Capacities and Volumes of Aqueous Solutions of Some Peptides that Model Side-chains of Proteins
Hedwig, Gavin R.
, p. 2761 - 2768 (2007/10/02)
The partial molar volumes V2infinite, and partial molar heat capacities, Cp,2infinite, at infinite dilution have been determined for the tripeptides glycyl-L-isoleucylglycine, glycyl-DL-threonylglycine, glycyl-L
