Structural Characterization of the Amino- and Carboxy -Terminal Domains of Troponin C by High Pressure Nuclear Magnetic Resonance

Our main research objective is to investigate the effects of high pressure on the structure, stability, and dynamics of proteins. The application of pressure provides a unique method to reversibly unfold proteins. Pressure is a gentler method of denaturation than other more traditional methods and also has the added benefit of generating a more concise thermodynamic description of the system. In our lab, one- and two-dimensional proton nuclear magnetic resonance is utilized to observe pressure-induced conformational changes and to isolate possible folding intermediates in proteins. Other techniques, such as computer simulations, circular dichroism, and fluorescence, are also utilized to obtain additional information. Through the use of a variety of spectroscopic techniques, the stability and folding pathways of proteins can be characterized.

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

• Yu, Aimee Cu

Contributors dc:contributor

• Jonas, Ana
• Jonas, Jiri

• Chemistry, Biochemistry

Language dc:language

eng

Identifier

(MiAaPQ)AAI9990200

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/84921