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Fast Events in Protein Folding Initiated by Nanosecond Laser Photolysis

Jones, Colleen M. ; Henry, Eric R. ; Hu, Yi ; Chan, Chi-Kin ; Luck, Stan D. ; Bhuyan, Abani ; Roder, Heinrich ; Hofrichter, James ; Eaton, William A.

Proceedings of the National Academy of Sciences - PNAS, 1993-12, Vol.90 (24), p.11860-11864 [Periódico revisado por pares]

Washington, DC: National Academy of Sciences of the United States of America

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Título:
Fast Events in Protein Folding Initiated by Nanosecond Laser Photolysis
Autor: Jones, Colleen M. ; Henry, Eric R. ; Hu, Yi ; Chan, Chi-Kin ; Luck, Stan D. ; Bhuyan, Abani ; Roder, Heinrich ; Hofrichter, James ; Eaton, William A.
Assuntos: Amino Acid Sequence ; Animals ; Binding Sites ; Biological and medical sciences ; Biology ; Carbon Monoxide - metabolism ; Conformational dynamics in molecular biology ; Cytochrome c Group - chemistry ; Cytochrome c Group - metabolism ; Cytochromes ; Datasets ; Dichroism ; Fluorescence ; Fundamental and applied biological sciences. Psychology ; Guanidine ; Guanidines - pharmacology ; Heme - metabolism ; Horses ; Kinetics ; Lasers ; Ligands ; Methionine ; Molecular biophysics ; Optics ; Photolysis ; Physics ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Proteins ; Spectrophotometry ; Time Factors ; Wavelengths
É parte de: Proceedings of the National Academy of Sciences - PNAS, 1993-12, Vol.90 (24), p.11860-11864
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Descrição: Initiation of protein folding by light can dramatically improve the time resolution of kinetic studies. Here we present an example of an optically triggered folding reaction by using nanosecond photodissociation of the heme-carbon monoxide complex of reduced cytochrome c. The optical trigger is based on the observation that under destabilizing conditions cytochrome c can be unfolded by preferential binding of carbon monoxide to the covalently attached heme group in the unfolded state. Photodissociation of the carbon monoxide thus triggers the folding reaction. We used time-resolved absorption spectroscopy to monitor binding at the heme. Before folding begins we observe transient binding of both nonnative and native ligands from the unfolded polypeptide on a microsecond time scale. Kinetic modeling suggests that the intramolecular binding of methionine-65 and -80 is faster than that of histidine-26 and -33, even though the histidines are closer to the heme. This optical trigger should provide a powerful method for studying chain collapse and secondary structure formation in cytochrome c without any limitations in time resolution.
Editor: Washington, DC: National Academy of Sciences of the United States of America
Idioma: Inglês

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Fast Events in Protein Folding Initiated by Nanosecond Laser Photolysis

Jones, Colleen M. ; Henry, Eric R. ; Hu, Yi ; Chan, Chi-Kin ; Luck, Stan D. ; Bhuyan, Abani ; Roder, Heinrich ; Hofrichter, James ; Eaton, William A.

Washington, DC: National Academy of Sciences of the United States of America

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