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dc.contributor.authorHileman, R.E.
dc.contributor.authorJennings, R.N.
dc.contributor.authorLinhardt, Robert J.
dc.date1998
dc.date.accessioned2022-06-27T16:21:51Z
dc.date.available2022-06-27T16:21:51Z
dc.date.issued1998
dc.identifier.citationThermodynamic Analysis of Heparin Interaction with a Basic CyclicProtein Using Isothermal Titration Calorimetry, R.E. Hileman, R. N. Jennings,R.J. Linhardt, Biochemistry, 37, 15231-15237, 1998.
dc.identifier.urihttps://doi.org/10.1021/bi980212x
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5892
dc.descriptionBiochemistry, 37, 15231-15237
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.abstractBrain natriuretic peptide (BNP) was examined as part of a continuing study of the interaction of proteins and peptides with the glycosaminoglycan heparin. BNP was tentatively identified as a heparin-binding protein on the basis of its cyclic structure and the high frequency of the basic amino acid residues, lysine and arginine. Thermodynamic analysis using isothermal titration calorimetry confirmed heparin binding to BNP with a micromolar Kd. Surprisingly, despite the high frequency (22%) of basic residues in BNP, only a small portion of the free energy of this interaction resulted from ionic contributions under physiologic conditions. The contribution of polar amino acids, representing 28% of BNP, was next examined in a variety of different buffers. These experiments demonstrated the transfer of five protons from buffer to BNP on heparin binding, suggesting that hydrogen bonding between the polar residues of BNP and heparin is a major factor contributing to the free energy of BNP binding to heparin. Hydrophobic forces apparently play only a small role in binding. Heparin contains few nonpolar functional groups, and a positive change in heat capacity (DeltaCp = 1 kcal/mol) demonstrates the loss of polar residues on BNP-heparin binding.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/bi980212x
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleThermodynamic Analysis of Heparin Interaction with a Basic CyclicProtein Using Isothermal Titration Calorimetry
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/bi980212x
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)


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