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    Order out of complexity; protein structures that interact with heparin

    Author
    Mulloy, Barbara; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    Other Contributors
    Date Issued
    2001-09-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In 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/;
    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.
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    URI
    https://doi.org/10.1016/S0959-440X(00)00257-8; https://hdl.handle.net/20.500.13015/5849
    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;
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