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Resolving local structures and dynamics of proteins with 2D IR spectroscopy

21 September 2012

PhD ceremony: Mr. S. Roy, 11.00 uur, Academiegebouw, Broerstraat 5, Groningen

Dissertation: Resolving local structures and dynamics of proteins with 2D IR spectroscopy

Promotor(s): prof. J. Knoester

Faculty: Mathematics and Natural Sciences

Proteins are essential components of a living system as they perform many mechanical and bio-chemical functions that are needed for survival. For example, elastin provides elasticity and enzymes function as catalysts to activate most of the reactions in the living system.

A protein spontaneously folds into the most stable structure with minimum free energy, which is known as protein folding. It is important to understand how proteins fold, as folding into wrong structures leads to Alzheimer’s disease, Parkinson's disease, type II diabetes, and cancer. To investigate functions and folding of proteins one needs to know their structures.

Resolving protein structure at different steps of bio-chemical reactions or in a folding process is a great challenge. This is because these phenomena happen in a wide range of time scales which can be from 1/1000000000000000 of seconds (femtoseconds) to seconds. We have developed methodologies that allow to resolve proteins structures which are involved in ultrafast interconversions (time scale ~100000 femtoseconds). This is done by combining theories and computations with experiments that are performed using infrared lasers to probe molecular vibrations. The methodologies can be used to identify different intermediates and the time scales at which they interconvert in a reaction/folding pathway.

Last modified:15 September 2017 3.42 p.m.
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