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PMID: 8401233 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Thermodynamics of apocytochrome b5 unfolding.

Protein science : a publication of the Protein Society ·Vol. 2 ·No. 9 ·1993-09-00 ·Pages 1497-501

Pfeil W

Abstract

Apocytochrome b5 from rabbit liver was studied by scanning calorimetry, limited proteolysis, circular dichroism, second derivative spectroscopy, and size exclusion chromatography. The protein is able to undergo a reversible two-state thermal transition. However, transition temperature, denaturational enthalpy, and heat capacity change are reduced compared with the holoprotein. Apocytochrome b5 stability in terms of Gibbs energy change at protein unfolding (delta G) amounts to delta G = 7 +/- 1 kJ/mol at 25 degrees C (pH 7.4) compared with delta G = 25 kJ/mol for the holoprotein. Apocytochrome b5 is a compact, native-like protein. According to the spectral data, the cooperative structure is mainly based in the core region formed by residues 1-35 and 79-90. This finding is in full agreement with NMR data (Moore, C.D. & Lecomte, J.T.J., 1993, Biochemistry 32, 199-207).

MeSH Terms

Animals Apoproteins/chemistry Calorimetry Chemical Phenomena Chemistry, Physical Chromatography, Gel Circular Dichroism Cytochrome b Group/chemistry Cytochromes b Endopeptidases/metabolism Liver/chemistry Protein Folding Protein Structure, Secondary Rabbits Spectrophotometry Thermodynamics

Chemicals

Apoproteins Cytochrome b Group Cytochromes b Endopeptidases

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Pfeil W

Max-Delbrück-Center for Molecular Medicine, Berlin-Buch, Germany.

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23 references, click to expand

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Article Info

Journal

Protein science : a publication of the Protein Society

Abbr.

Protein Sci

ISSN

0961-8368

DOI

10.1002/pro.5560020914

Published

1993-09-00

Pages

1497-501

Language

English

Region

United States

NLM ID

9211750

PMCID

PMC2142466

Subset

External Links

PubMed source DOI: 10.1002/pro.5560020914 PMC Full Text View journal details

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