Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives.

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Abstract Text:

H Sano,S Takahashi,T Iio,

We studied Ca2+-dependent structural change of rabbit skeletal troponin C (TnC)-melittin (ME) complex as a model of TnC-troponin I complex. In previous study, we found that the distance between Met-25 and Cys-98 of TnC in TnC-ME complex increased upon binding of Ca2+ to TnC [H. Sano and T. Iio (1995) J. Biochem. 118, 996-1000]. In this study, we used a fluorescence energy transfer method. As a fluorescent donor, we used the tryptophan residue in four melittin derivatives, in which residue 2, 5, 8, or 13 was replaced with tryptophan. As acceptor, we used dansylaziridine (DANZ) bound to Met-25 of TnC, or N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine (1,5-I-AEDANS) bound to Cys-98 of TnC. For all TnCDANZ-ME complexes, the donor-acceptor distance (11.9-17.7 A) did not remarkably depend on Mg2+ or Ca2+ binding of TnC or on the position of tryptophan in ME derivatives. The same results were obtained for TnCAEDANS-ME complexes in the absence of Ca2+ (distance 15.2-21.7 A). But in the presence of Ca2+, tryptophan residues in the central region of ME were near to Cys-98 of TnC (distance much less than 10.4 A). Based on these results, we conclude that ME is enfolded by the N- and C-lobes of TnC, and the ME rod is almost perpendicular to a line connecting Met-25 and Cys-98 of TnC. The position of the ME rod shifts upon binding of Ca2+ to TnC.

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Publishing Authors By Initials

H Sano,S Takahashi,T Iio,

For similar macromolecular substances: polymers: biopolymers: microfilament proteins: troponin: troponin c research abstracts see: macromolecular substances: polymers: biopolymers: microfilament proteins: troponin: troponin c research

PUBMED ID PMID:

MEDLINE DATE:

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 124

Page Numbers: 602-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1998

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Keywords Mesh Terms:

KEYWORDS: Troponin C

MESH TERMS: chemistry

Chemical & Substance for Abstract: Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives. Information

Substance Name: Melitten

Registry Number: 20449-79-0

Grant and Affiliation Information for Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives.

AFFILIATION: Department of Physics, Faculty of Science, Nagoya University, Chikusa-ku, Nagoya, Aichi, 464-8602, Japan. zetha@white.plala.or.jp

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives Related Publications

• 11C-glucose metabolism in manic and depressed patients.
• Brain tumors with ipsilateral cerebral hemiatrophy.
• Conformational change of skeletal muscle troponin.
• Conformational change of troponin T induced by calcium binding to troponin C.
• Fluorescence energy transfer of complexes of skeletal muscle troponin C and melittin derivatives.
• Fluorescence energy transfer study of troponin C-melittin complex.
• Hypometabolism and dipole localization in hemimegalencephaly: a case report.
• Kinetics of the conformational change of skeletal troponin C induced by Ca2+-Mg2+ exchange at the high-affinity Ca2+-binding sites.
• MR differentiation of hepatocellular carcinoma from cavernous hemangioma: complementary roles of FLASH and T2 values.
• Magnetic resonance imaging of clival chordomas.
• Melittin-binding of troponin C.
• Positron emission tomography in systemic lupus erythematosus: relation of cerebral vasculitis to PET findings.
• Regenerating nodules of liver cirrhosis: MR imaging with pathologic correlation.
• Reversible symmetrical white matter low attenuation in rubella encephalitis. Both in X-ray CT and 11C-glucose positron emission tomography.
• Static and kinetic studies of calmodulin and melittin complex.
• Static and kinetic studies on rabbit skeletal muscle troponin.
• [Primary urothelial carcinoma of the prostate: a case of spread along ducts and into seminal vesicles]