Conformational stability of cytochrome C probed by optical spectroscopy.

Abstract:

:Over the last 50 years cytochrome c has been used as a model system for studying electron transfer and protein folding processes. Recently, convincing evidence has been provided that this protein is also involved in other biological processes such as the apoptosis and α-synuclein aggregation. Numerous lines of evidence suggest that the diversity of the functional properties of cytochrome c is linked to its conformational plasticity. This chapter introduces circular dichroism and absorption spectroscopy, as an ideal tool to explore this protein's conformational in solution. Besides assisting in distinguishing different conformations and in obtaining the equilibrium thermodynamics of the transitions between them, the two spectroscopies can also be used to explore details of heme-protein interaction, for example, the influence of the external electric field on the prosthetic heme group.

journal_name

Methods Enzymol

journal_title

Methods in enzymology

authors

Schweitzer-Stenner R,Hagarman A,Verbaro D,Soffer JB

doi

10.1016/S0076-6879(09)66006-7

subject

Has Abstract

pub_date

2009-01-01 00:00:00

pages

109-53

eissn

0076-6879

issn

1557-7988

pii

S0076-6879(09)66006-7

journal_volume

466

pub_type

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