Persistent Link:
http://hdl.handle.net/10150/291684
Title:
Retroevolution of the structure of lambda Cro
Author:
LeFevre, Kelly
Issue Date:
2002
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:
The Cro protein from bacteriophage λ has a dimeric mixed α+β fold which evolved from an ancestral monomeric all-α fold. Monomeric mixed α+β structures may have been intermediates in this process. A monomeric variant of λ Cro incorporating A33W and F58D mutations has been identified and characterized. These mutations involve large changes in side chain size, and were predicted by modeling to disrupt the dimer interface while increasing the thermodynamic stability of the monomer. This combination of mutations does lower the λ Cro dissociation constant by a factor of at least 1,000, while maintaining the protein's secondary structure content. The A33W and F58D mutations also increase the maximal monomer thermal stability of λ Cro by approximately 12 degrees. The A33W/F58D Cro variant shows the plausibility of monomeric mixed α+β intermediates in the evolution of λ Cro, and shows that mutations at these positions could have been critical for evolution of the dimer.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Biology, Molecular.; Chemistry, Biochemistry.; Biophysics, General.
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College; Molecular and Cellular Biology
Degree Grantor:
University of Arizona
Advisor:
Cordes, Matthew H. J.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleRetroevolution of the structure of lambda Croen_US
dc.creatorLeFevre, Kellyen_US
dc.contributor.authorLeFevre, Kellyen_US
dc.date.issued2002en_US
dc.publisherThe University of Arizona.en_US
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_US
dc.description.abstractThe Cro protein from bacteriophage λ has a dimeric mixed α+β fold which evolved from an ancestral monomeric all-α fold. Monomeric mixed α+β structures may have been intermediates in this process. A monomeric variant of λ Cro incorporating A33W and F58D mutations has been identified and characterized. These mutations involve large changes in side chain size, and were predicted by modeling to disrupt the dimer interface while increasing the thermodynamic stability of the monomer. This combination of mutations does lower the λ Cro dissociation constant by a factor of at least 1,000, while maintaining the protein's secondary structure content. The A33W and F58D mutations also increase the maximal monomer thermal stability of λ Cro by approximately 12 degrees. The A33W/F58D Cro variant shows the plausibility of monomeric mixed α+β intermediates in the evolution of λ Cro, and shows that mutations at these positions could have been critical for evolution of the dimer.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectBiology, Molecular.en_US
dc.subjectChemistry, Biochemistry.en_US
dc.subjectBiophysics, General.en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorCordes, Matthew H. J.en_US
dc.identifier.proquest1409488en_US
dc.identifier.bibrecord.b42813542en_US
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