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dc.contributor.authorMikhailov, Dmitri
dc.contributor.authorMayo, Kevin H.
dc.contributor.authorPervin, Azra
dc.contributor.authorLinhardt, Robert J.
dc.date1996
dc.date.accessioned2022-06-27T17:13:46Z
dc.date.available2022-06-27T17:13:46Z
dc.date.issued1996-04-15
dc.identifier.citation13C-NMR Relaxation Study of Heparin Disaccharide with Tripeptides GRG and GKG, D. Mikhailov, K. Mayo, R.J. Linhardt, A. Pervin Biochemical Journal, 315, 447-454, 1996.
dc.identifier.issn2646021
dc.identifier.urihttps://doi.org/10.1042/bj3150447
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5938
dc.descriptionBiochemical Journal, 315, 447-454
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractHeparin is a polydisperse sulphated copolymer consisting mostly of 1-->4 linked glucosamine and uronic acid residues, i.e. 2-deoxy-2-sulphamido-D-glucopyranose 6-sulphate and L-idopyranosyluronic acid 2-sulphate. 13C NMR has been used to study the interactions of heparinase-derived and purified heparin disaccharide with N- and C-terminally-blocked tripeptides GRG and GKG. Titration of the disaccharide with peptide indicates that GRG binds the disaccharide more strongly than does GKG, with interactions in either case being stronger at uronate ring positions. In the presence of GRG, a carboxylate pKa depression suggests electrostatic interactions between the arginine guanidinium group and the uronate carboxylate group. 13C relaxation data have been acquired for all disaccharide and peptide carbons in the presence and absence of GRG and GKG. 13C relaxation rates for the disaccharide are significantly faster in the presence of peptide, especially with GRG. Analysis of these relaxation data has been done in terms of molecular diffusion constants, D [symbol: see text] and D parallel, and an angle alpha between D parallel and a molecular frame defined by the moment of inertia tensor calculated for an internally rigid disaccharide. Disaccharide conformational space in these calculations has been sampled for both uronate half-chair forms (2H1 and 1H2) and over a range of glycosidic bond angles defined by motional order parameters and inter-residue nuclear Overhauser effects (+/- 30 degree from the average). In the absence of peptide, the ratio D [symbol: see text] /D parallel falls between 0.4 and 0.7; therefore molecular diffusion occurs preferentially about D parallel, which runs through both disaccharide rings. In the presence of peptide, D [symbol: see text] /D parallel is decreased, indicating that GRG is oriented along D parallel and proximal to the uronic acid ring. A model for this is shown.
dc.description.sponsorshipNational Institute of General Medical Sciences
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1042/bj3150447
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemical Journal
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.title13C-NMR Relaxation Study of Heparin Disaccharide with Tripeptides GRG and GKG
dc.typeArticle
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dcterms.isVersionOfhttps://doi.org/10.1042/bj3150447
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages447-454
rpi.description.volume315


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