Dynamic Aspects of Protein Structure - a Fluorescence Spectroscopic Approach

Structural fluctuations of proteins were investigated using steady state and time-resolved fluorescence techniques. High resolution anisotropy decay measurements were used to test the findings of molecular dynamics calculations on tryptophan and tyrosine residues in lysozyme and bovine pancreatic trypsin inhibitor (BPTI) respectively. Anisotropy decays measured over a large viscosity range failed to observe the very fast rotational modes of intrinsic fluorophores calculated in the molecular dynamics approach. The experimental rotational correlation times for the tryptophan residues in lysozyme were approximately 1 nanosecond at room temperature in aqueous solution and approximately 0.6 nanosecond for the tyrosine residues in BPTI.

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

2014

Author dc:creator

• Marriott, Gerard Joseph

• Chemistry, Biochemistry

Identifier

(UMI)AAI8711832

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/70562