Literature DB >> 6149548

Amino acid sequence of bovine heart coupling factor 6.

J K Fang, J W Jacobs, B I Kanner, E Racker, R A Bradshaw.   

Abstract

The amino acid sequence of bovine heart mitochondrial coupling factor 6 (F6) has been determined by automated Edman degradation of the whole protein and derived peptides. Preparations based on heat precipitation and ethanol extraction showed allotypic variation at three positions while material further purified by HPLC yielded only one sequence that also differed by a Phe-Thr replacement at residue 62. The mature protein contains 76 amino acids with a calculated molecular weight of 9006 and a pI of approximately equal to 5, in good agreement with experimentally measured values. The charged amino acids are mainly clustered at the termini and in one section in the middle; these three polar segments are separated by two segments relatively rich in nonpolar residues. Chou-Fasman analysis suggests three stretches of alpha-helix coinciding (or within) the high-charge-density sequences with a single beta-turn at the first polar-nonpolar junction. Comparison of the F6 sequence with those of other proteins did not reveal any homologous structures.

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Year:  1984        PMID: 6149548      PMCID: PMC391978          DOI: 10.1073/pnas.81.21.6603

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  17 in total

1.  Coupling factors--an overview.

Authors:  D R Sanadi; S Joshi
Journal:  Methods Enzymol       Date:  1979       Impact factor: 1.600

2.  Preparation and characterization of homogeneous coupling factor 6 from bovine heart mitochondria.

Authors:  B I Kanner; R Serrano; M A Kandrach; E Racker
Journal:  Biochem Biophys Res Commun       Date:  1976-04-19       Impact factor: 3.575

Review 3.  Empirical predictions of protein conformation.

Authors:  P Y Chou; G D Fasman
Journal:  Annu Rev Biochem       Date:  1978       Impact factor: 23.643

4.  Purification of coupling factor B.

Authors:  S Joshi; R R Sanadi
Journal:  Methods Enzymol       Date:  1979       Impact factor: 1.600

5.  Purification and properties of a new coupling factor required for oxidative phosphorylation in silicotungstate-treated submitochondrial particles.

Authors:  J M Fessenden-Raden
Journal:  J Biol Chem       Date:  1972-04-25       Impact factor: 5.157

6.  Partial resolution of the enzymes catalyzing oxidative phosphorylation. XVII. Further resolution of the rutamycin-sensitive adenosine triphosphatase.

Authors:  B Bulos; E Racker
Journal:  J Biol Chem       Date:  1968-07-25       Impact factor: 5.157

7.  Studies on the mitochondrial adenosine triphosphatase system. IV. Purification and characterization of the oligomycin sensitivity conferring protein.

Authors:  D H MacLennan; A Tzagoloff
Journal:  Biochemistry       Date:  1968-04       Impact factor: 3.162

8.  Partial resolution of the enzymes catalyzing oxidative phosphorylation. XXIV. A factor required for the binding of mitochondrial adenosine triphosphatase to the inner mitochondrial membrane.

Authors:  A F Knowles; R J Guillory; E Racker
Journal:  J Biol Chem       Date:  1971-04-25       Impact factor: 5.157

9.  Amino-terminal analysis of polypeptide using dimethylaminoazobenzene isothiocyanate.

Authors:  J Y Chang
Journal:  Anal Biochem       Date:  1980-03-01       Impact factor: 3.365

10.  Identity of coupling factor 2 and factor B.

Authors:  E Racker; J M Fessenden-Raden; M A Kandrach; K W Lam; D R Sanadi
Journal:  Biochem Biophys Res Commun       Date:  1970-12-24       Impact factor: 3.575

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  1 in total

Review 1.  Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.

Authors:  E Schneider; K Altendorf
Journal:  Microbiol Rev       Date:  1987-12
  1 in total

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