Journal article
Partially formed native tertiary interactions in the A-state of cytochrome c
Journal of molecular biology, v 289(3), pp 639-644
11 Jun 1999
PMID: 10356334
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Considerable insight into protein structure, stability, and folding has been obtained from studies of non-native states. We have studied the extent of native tertiary contacts in one such molecule, the A-state of yeast iso-1-ferricytochrome
c. Previously, we showed that the interface between the N and C-terminal helices is completely formed in the A-state. Here, we focus on interactions essential for forming the heme pocket of eukaryotic cytochromes
c. To determine the extent of these interactions, we used saturation mutagenesis at the evolutionarily invariant residue leucine 68, and measured the free energy of denaturation for the native states and the A-states of functional variants. We show that, unlike the interaction between the terminal helices, the native interactions between the 60s helix and the rest of the protein are not completely formed in the A-state.
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Details
- Title
- Partially formed native tertiary interactions in the A-state of cytochrome c
- Creators
- Daniel R. Hostetter - University of North Carolina at Chapel HillGresham T. Weatherly - University of North Carolina at Chapel HillJames R. Beasley - University of North Carolina at Chapel HillKara Bortone - University of North Carolina at Chapel HillDavid S. Cohen - University of North Carolina at Chapel HillShelly A. Finger - University of North Carolina at Chapel HillPhilip Hardwidge - University of North Carolina at Chapel HillDionysios S. Kakouras - University of North Carolina at Chapel HillAleister J. Saunders - University of North Carolina at Chapel HillSonja K. Trojak - University of North Carolina at Chapel HillJennifer C. Waldner - University of North Carolina at Chapel HillGary J. Pielak - University of North Carolina at Chapel Hill
- Publication Details
- Journal of molecular biology, v 289(3), pp 639-644
- Publisher
- Elsevier
- Number of pages
- 6
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biology
- Web of Science ID
- WOS:000081109800016
- Scopus ID
- 2-s2.0-0033546385
- Other Identifier
- 991021448155004721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology