Persistent Link:
http://hdl.handle.net/10150/578419
Title:
Geometry Of Alpha And Beta Protein Structures
Author:
Shah, Aalok K.
Issue Date:
2015
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Proteins have a wide array of essential functions: from serving as enzymatic catalysts to protecting the immune system as antibodies. Proteins spontaneously self-organize into specific, folded structures determined by their amino acid sequences and the interaction between molecular forces. Since the 3-dimensional structure into which they fold often relates to the specific function of the protein, much effort has been directed towards methods to predict the folded structure from a given sequence, with the hope of being able to understand protein functions from sequence information. The protein folding problem can be summarized as the attempt to understand the relationship between a protein sequence and a protein's geometric shape, or fold. Thus, there are two principal problems: given a sequence, what 3-dimensional form will the protein take (forward problem), and given a particular fold, what sequence or sequences code for that form (the inverse problem). In this work, models that represent folds as continuous structures are explored. Models of the two prevalent motifs in protein folds, α helices and β barrels, are developed using axially deformed tubes and surfaces of revolution. These models are then analyzed and used to develop coordinate models of known and unknown structures.
Type:
text; Electronic Dissertation
Keywords:
coiled coils; continuous; geometry; proteins; Applied Mathematics; beta barrel
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Applied Mathematics
Degree Grantor:
University of Arizona
Advisor:
Hausrath, Andrew; Tabor, Michael

Full metadata record

DC FieldValue Language
dc.language.isoen_USen
dc.titleGeometry Of Alpha And Beta Protein Structuresen_US
dc.creatorShah, Aalok K.en
dc.contributor.authorShah, Aalok K.en
dc.date.issued2015en
dc.publisherThe University of Arizona.en
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en
dc.description.abstractProteins have a wide array of essential functions: from serving as enzymatic catalysts to protecting the immune system as antibodies. Proteins spontaneously self-organize into specific, folded structures determined by their amino acid sequences and the interaction between molecular forces. Since the 3-dimensional structure into which they fold often relates to the specific function of the protein, much effort has been directed towards methods to predict the folded structure from a given sequence, with the hope of being able to understand protein functions from sequence information. The protein folding problem can be summarized as the attempt to understand the relationship between a protein sequence and a protein's geometric shape, or fold. Thus, there are two principal problems: given a sequence, what 3-dimensional form will the protein take (forward problem), and given a particular fold, what sequence or sequences code for that form (the inverse problem). In this work, models that represent folds as continuous structures are explored. Models of the two prevalent motifs in protein folds, α helices and β barrels, are developed using axially deformed tubes and surfaces of revolution. These models are then analyzed and used to develop coordinate models of known and unknown structures.en
dc.typetexten
dc.typeElectronic Dissertationen
dc.subjectcoiled coilsen
dc.subjectcontinuousen
dc.subjectgeometryen
dc.subjectproteinsen
dc.subjectApplied Mathematicsen
dc.subjectbeta barrelen
thesis.degree.namePh.D.en
thesis.degree.leveldoctoralen
thesis.degree.disciplineGraduate Collegeen
thesis.degree.disciplineApplied Mathematicsen
thesis.degree.grantorUniversity of Arizonaen
dc.contributor.advisorHausrath, Andrewen
dc.contributor.advisorTabor, Michaelen
dc.contributor.committeememberHausrath, Andrewen
dc.contributor.committeememberTabor, Michaelen
dc.contributor.committeememberVenkataramani, Shankaren
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