Author
Mulloy, Barbara; Linhardt, Robert J.
Other Contributors
Date Issued
2001-09-01
Subject
Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
Degree
Terms of Use
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Full Citation
Order out of complexity; protein structures that interact with heparin, B. Mulloy, R.J. Linhardt, Current Opinions in Structural Biology, 11, 623-628, 2001.
Abstract
Many proteins of widely differing functionality and structure are capable of binding heparin. Structural characterisations of the many types of such complexes are being reported in ever-increasing number and at improved resolution. Several crystal structures of complexes formed through the interaction of heparin-derived oligosaccharides with one or more protein partners have been described.;
Description
Current Opinions in Structural Biology, 11, 623-628; Note : 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.
Department
The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
Relationships
The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Current Opinion in Structural Biology; https://harc.rpi.edu/;
Access
https://login.libproxy.rpi.edu/login?url=https://doi.org/10.1016/S0959-440X(00)00257-8;
