Journal article
Conformational stability of cytochrome C probed by optical spectroscopy
Methods in enzymology, Vol.466, pp.109-153
2009
PMID: 21609860
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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.
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Details
- Title
- Conformational stability of cytochrome C probed by optical spectroscopy
- Creators
- Reinhard Schweitzer-Stenner - Department of Chemistry, Drexel University, Philadelphia, Pennsylvania, USAAndrew HagarmanDaniel VerbaroJonathan B Soffer
- Publication Details
- Methods in enzymology, Vol.466, pp.109-153
- Publisher
- Elsevier; United States
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemistry
- Identifiers
- 991014878334704721
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- Biochemical Research Methods
- Biochemistry & Molecular Biology