High Pressure Protein Denaturation: Description of a High Pressure Intermediate and Effects of Mutations on Pressure Stability

Four mutations were also examined to determine how specific packing defects affect high pressure denaturation. Mutations were made in three positions in the core to determine how the position contributes to changes in stability. Also, charged and oversized residues were introduced into the core to determine how particular types of defects affect the pressure stability of the native and high pressure intermediate states. The effects of mutation are shown to be more dependent on the nature of the mutation, with charge burial mutations being the most deleterious given that all positions are buried in the AGH core.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2015

Author dc:creator

• Bondos, Sarah Elizabeth

Contributors dc:contributor

• Sligar, Stephen G.
• Jonas, Jiri

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI9912197

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84895