The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c.

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Research Abstract Details 

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The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Abstract Text:

Oleg Y Dmitriev,Robert H Fillingame,

We have tested the role of the polar loop of subunit c of the Escherichia coli ATP synthase in stabilizing the hairpin structure of this protein. The structure of the c(32-52) peptide corresponding to the cytoplasmic region of subunit c bound to the dodecylphosphocholine micelles was solved by high-resolution NMR. The region comprising residues 41-47 forms a well-ordered structure rather similar to the conformation of the polar loop region in the solution structure of the full-length subunit c and is flanked by short alpha-helical segments. This result suggests that the rigidity of the polar loop significantly contributes to the stability of the hairpin formed by the two helices of subunit c. This experimental system may be useful for NMR studies of interactions between subunit c and subunits gamma and epsilon, which together form the rotor of the ATP synthase.

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Publishing Authors By Initials

OY Dmitriev,RH Fillingame,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, secondary research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: molecular structure: molecular conformation: protein conformation: protein structure, secondary research

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The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Protein science : a publication of the Protein Soc

VOLUME: 16

Page Numbers: 2118-22

Journal Abbreviation: Protein Sci.

ISSN: 0961-8368

DAY: 31

MONTH: 08

YEAR: 2007

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9211750

The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Keywords Mesh Terms:

KEYWORDS: Protein Structure, Secondary

MESH TERMS: chemistry

Chemical & Substance for Abstract: The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c. Information

Substance Name: Bacterial Proton-Translocating ATPases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c.

AFFILIATION: Department of Biochemistry, University of Saskatchewan, Saskatoon, Saskatchewan, Canada. Oleg.Dmitriev@usask.ca

Country: United States

AGENCY: United States NIGMS

GRANT: GM23105

ACRONYM: GM

MEDLINETA: Protein Sci

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• The rigid connecting loop stabilizes hairpin folding of the two helices of the ATP synthase subunit c.