Show simple item record

dc.rights.licenseRestricted to current Rensselaer faculty, staff and students. Access inquiries may be directed to the Rensselaer Libraries.
dc.contributorLinhardt, Robert J.
dc.contributorHahn, Juergen
dc.contributorGilbert, Ryan
dc.contributorWang, Chunyu
dc.contributorGarcia, Angel E.
dc.contributor.authorJanke, Jonathan Joel
dc.date.accessioned2021-11-03T09:22:53Z
dc.date.available2021-11-03T09:22:53Z
dc.date.created2021-02-22T15:34:42Z
dc.date.issued2020-08
dc.identifier.urihttps://hdl.handle.net/20.500.13015/2639
dc.descriptionAugust 2020
dc.descriptionSchool of Engineering
dc.description.abstractAs a member of the glycosaminoglycan family of biomolecules, heparin is a highly negatively charged polysaccharide, best known for its anticoagulant activity. The pentasaccharide sequence of heparin responsible for anticoagulant activity is ArixtraTM (also known as fondaparinux), which is an important drug. While the function of ArixtraTM is well characterized, its conformational ensemble is less well known. Thus, the purpose of Chapters 2 and 3 of this thesis is to characterize the conformational ensemble of ArixtraTM using molecular dynamics simulations, with a view towards the best method to simulating heparin (Chapter 2) and the effect of sulfation on the conformational ensemble of ArixtraTM. Chapter 4 is then dedicated to characterizing the heparin binding site of a bone protein known as sclerostin using molecular dynamics simulations. The outcome of this thesis is to provide an in depth understanding of heparin’s conformational ensemble and how it relates to the function of heparin in anticoagulation as well as providing a method to find and characterize heparin binding sites for activities of heparin beyond anticoagulation.
dc.language.isoENG
dc.publisherRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofRensselaer Theses and Dissertations Online Collection
dc.subjectBiomedical engineering
dc.titleSimulations of heparin : force fields, sequences, and interactions with sclerostin
dc.typeElectronic thesis
dc.typeThesis
dc.digitool.pid180412
dc.digitool.pid180413
dc.digitool.pid180414
dc.rights.holderThis electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
dc.description.degreePhD
dc.relation.departmentDept. of Biomedical Engineering


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record