An Unbiased Approach on The Conformational Dynamics of In-Solution Fibrinogen and Its Physiological Implications.

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dc.contributorÅžen, Mehmet
dc.contributorSirrieh, Rita
dc.contributorCruz, Miguel
dc.contributor.authorEsparza Pinelo, Jose E.
dc.date.accessioned2022-07-11T14:40:43Z
dc.date.available2022-07-11T14:40:43Z
dc.date.issued2022-04-29
dc.description.abstractBy itself, Fibrinogen (Fng) stands out as one of the most complex hematopoietic proteins in the cardiovascular system for multiple species in nature. Upon its activation and further cascade mechanisms, Fng can polymerize into fibrin and contribute to blood clot formation and substantial growth. Fng’s interactions with fibrinolytic proteins aggregate into a conglomerate of different fragments in blood bodily mechanisms. Any form of dysregulation in any of these pathways can lead to several complications not only within the cardiovascular system but throughout the entirety of the body. Understanding the crux of Fng’s functions and interactions with itself along with other proteins ultimately can be traced back to its inherent dynamic structure. In this study, I aim to probe the intrinsic flexibility that is beset on Fng by way of its multi-domain composition, allowing it to withstand incredible mechanical forces as well as being highly dynamic in its physiological form. Thus, extending the key biological concept that structure and flexibility that comes with it determine functions. Through an unbiased approach by implementing protein structural studies as well as computational dynamic simulations, in-solution Fng dynamics were studied in their totality.
dc.description.departmentBiology and Biochemistry, Department of
dc.description.departmentHonors College
dc.identifier.urihttps://hdl.handle.net/10657/10513
dc.language.isoen
dc.relation.ispartofSenior Honors Theses
dc.rightsThe author of this work is the copyright owner. UH Libraries and the Texas Digital Library have their permission to store and provide access to this work. Further transmission, reproduction, or presentation of this work is prohibited except with permission of the author(s).
dc.subjectFibrinogen
dc.subjectFibrin
dc.subjectin-solution
dc.subjectcoiled coil domain
dc.subjectglobular regions
dc.subjectHDX-MS
dc.subjectNegative Stain Electromagnetic Imaging
dc.subjectSmall Angle X-ray Scattering
dc.subjectX-ray crystallography
dc.subjectconformational dynamics
dc.subjectcoagulation
dc.subjectplatelet aggregation.
dc.titleAn Unbiased Approach on The Conformational Dynamics of In-Solution Fibrinogen and Its Physiological Implications.
dc.typeHonors Thesis
dc.type.dcmiText
dcterms.accessRightsThe full text of this item is not available at this time because the student has placed this item under an embargo for a period of time. The Libraries are not authorized to provide a copy of this work during the embargo period.
thesis.degree.collegeCollege of Natural Sciences and Mathematics
thesis.degree.levelBachelors
thesis.degree.nameBachelor of Science

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