Rational design of tropomyosin mutants the tni-binding site (1995)
- Authors:
- Autor USP: REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquimica e Biologia Molecular
- Publisher place: Sao Paulo
- Date published: 1995
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reuniao Anual da Sociedade Brasileira de Bioquimica e Biologia Molecular
-
ABNT
CORREIA, R G; REINACH, Fernando de Castro. Rational design of tropomyosin mutants the tni-binding site. Anais.. Sao Paulo: Sociedade Brasileira de Bioquimica e Biologia Molecular, 1995. -
APA
Correia, R. G., & Reinach, F. de C. (1995). Rational design of tropomyosin mutants the tni-binding site. In Programa e Resumos. Sao Paulo: Sociedade Brasileira de Bioquimica e Biologia Molecular. -
NLM
Correia RG, Reinach F de C. Rational design of tropomyosin mutants the tni-binding site. Programa e Resumos. 1995 ; -
Vancouver
Correia RG, Reinach F de C. Rational design of tropomyosin mutants the tni-binding site. Programa e Resumos. 1995 ; - Analysis of the metal-induced conformational change in myosin with a monoclonal antibody to light chain two
- Engineering the calcium binding sites of myosin light chain and skeletal muscle
- Construction of a regulatory myosin light chain capable regulation of myosin
- Sequences of complete cdnas encoding four variants of chicken skeletal muscle troponin t
- Sequenciamento de dna
- Cloning , expression and site-directed mutagenesis of chicken skeletal muscle troponin c
- Glu 88 is involved in troponin - c interactions with the regulatory proteins of the thin filament in vertebrate skeletal muscle fibers
- Hybrid myosin regulatory light chain containing a troponin c metal binding site
- Human myosin binding protein h (mybp-h): complete sequence, genomic organization, and chromosomal localization
- Functional alpha-tropomyosin produced in escherichia coli . A dipeptide extension can substitute the amino-terminal acetyl group
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