Transient intermediate units in protein folding / Linh Duy Hoang.

Format:

Book

Manuscript

Microformat

Thesis/Dissertation

Author/Creator:

Hoang, Linh Duy.

Contributor:

Englander, Sol Walter, advisor.

University of Pennsylvania.

Language:

English

Subjects (All):

Penn dissertations--Biochemistry and molecular biophysics.

Biochemistry and molecular biophysics--Penn dissertations.

Biochemistry and Molecular Biophysics.

Academic Dissertations as Topic.

Medical Subjects:

Biochemistry and Molecular Biophysics.

Academic Dissertations as Topic.

Local Subjects:

Penn dissertations--Biochemistry and molecular biophysics.

Biochemistry and molecular biophysics--Penn dissertations.

Physical Description:

xvi, 245 pages : illustrations (some color) ; 29 cm

Production:

2003.

Summary:

How a polypeptide chain folds into its final native structure as it comes off the ribosome is the final step in the Central Dogma of biology. A better understanding of this fundamental process may have implications for structure prediction, folding diseases and protein design. Cytochrome c is a well-studied protein folding model. Cytochrome c structure can be broken down into cooperative units of secondary structure, detectable by hydrogen exchange. Cytochrome c folds through the sequential acquisition of these structural units. In two-state folding, these units fail to accumulate and are normally undetectable. This work describes the development of a technique that detects not only the transient population of these units but also the "hidden" kinetic barriers that separate them. The folding pathway of cytochrome c seems to have functional importance. Major conformational changes, such as the alkaline transition, appear to occur through the folding pathway. To facilitate further studies, a recombinant cytochrome c was expressed with high yields in E. coli. Initial hydrogen exchange studies of the modified recombinant protein are described. The last section discusses the generalization of the nucleation-sequential stabilization model.

Notes:

Adviser: Sol Walter Englander.

Thesis (Ph.D. in Biochemistry and Molecular Biophysics) -- University of Pennsylvania, 2003.

Includes bibliographical references and index.

Local Notes:

University Microfilms order no.: 3087412.

OCLC:

244972938