Investigation of possible driving forces on counter-intuitive thermal collapse of intrinsically disordered proteins

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dc.access.optionRestricted Campus Access Only
dc.contributor.advisorBurns, Colin Sanderson
dc.contributor.authorCormier, Zachary
dc.contributor.departmentChemistry
dc.date.accessioned2017-01-11T19:42:58Z
dc.date.available2018-01-23T17:31:57Z
dc.date.created2016-12
dc.date.issued2016-08-18
dc.date.submittedDecember 2016
dc.date.updated2017-01-11T14:30:59Z
dc.degree.departmentChemistry
dc.degree.disciplineMS-Chemistry
dc.degree.grantorEast Carolina University
dc.degree.levelMasters
dc.degree.nameM.S.
dc.description.abstractIntrinsically disordered proteins are an emerging class of proteins that contain no secondary or tertiary structure. Through bioinformatics studies it has been predicted that a third of the human proteome consists of proteins containing intrinsic disorder. It was originally thought that a well-defined three dimensional structure was a prerequisite for function. However, this new class of proteins has been found to perform a variety of functions which has helped to establish new ways of classifying protein function. Intrinsically disordered proteins can undergo disorder-to-order transitions under different environmental factors. Of particular interest is a "turned out" response to increasing temperature. These proteins undergo a thermal collapse which is counter-intuitive to the traditional notion of protein folding and denaturation which states that under increasing temperature a protein should go into a more extended conformation. The reason for this counter-intuitive thermal collapse is still unknown. The goal of our research was to find the main driving force behind thermal collapse of intrinsically disordered proteins. Utilizing circular dichroism, the structure and transitions of four polypeptides (prothymosin-alpha (50-89)N50W, scrambled prothymosin-alpha (50-89), scrambled prothymosin-alpha (50-89) in 1M KF, and a polyE peptide) where analyzed under increasing temperatures of 25 [degrees]C to 80 [degrees]C to observe the possible effects of net charge, hydrophobicity, and sequence specificity on the thermal collapse of intrinsically disordered proteins. All peptides collapsed to similar degrees under increasing temperatures. The ionic strength condition appeared to be more collapsed than the non-salt condition indicating net charge as a major player. The hydrophobic effect also appears to play a major role in counter-intuitive collapse which may be attributed to the change in hydrophobicity of polar side chains.
dc.embargo.lift2018-01-11
dc.format.mimetypeapplication/pdf
dc.identifier.urihttp://hdl.handle.net/10342/6000
dc.language.isoen
dc.publisherEast Carolina University
dc.subjectIntrinsically Disordered Proteins
dc.subjectCounter-Intuitive Thermal Collapse
dc.subject.lcshProteins--Analysis
dc.subject.lcshCircular dichroism
dc.subject.lcshPolypeptides
dc.titleInvestigation of possible driving forces on counter-intuitive thermal collapse of intrinsically disordered proteins
dc.typeMaster's Thesis
dc.type.materialtext

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