A Survey of Beta-Sheet Folding: WW Domains With Zinc Fingers and Membrane Peptides

This work describes the present state of folding research involving small, fast-folding protein systems. By perturbing a WW domain sequence with side-chain mutations, truncations, amide-to-ester exchanges, and loop rearrangements we find that loop structures can dictate the folding dynamics of this model beta-sheet protein. We then report on a synthetic zinc-finger peptide used to bridge the gap between experimental and theoretical protein folding research. To complete our work we summarize ongoing research on the membrane interactions of a small alpha-helical peptide.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biophysics and Computational Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Nguyen, Houbi Tung Thanh

Contributors dc:contributor

• Martin Gruebele

• Biophysics, General

Language dc:language

eng

Identifier

(MiAaPQ)AAI3160934

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/85441