Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin (2001)
- Authors:
- USP affiliated authors: FARAH, SHAKER CHUCK - IQ ; REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Source:
- Título: Programa e resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
VIDSIUNAS, E. K. e FARAH, Chuck Shaker e REINACH, Fernando de Castro. Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin. 2001, Anais.. São Paulo: SBBq, 2001. . Acesso em: 13 fev. 2026. -
APA
Vidsiunas, E. K., Farah, C. S., & Reinach, F. de C. (2001). Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin. In Programa e resumos. São Paulo: SBBq. -
NLM
Vidsiunas EK, Farah CS, Reinach F de C. Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin. Programa e resumos. 2001 ;[citado 2026 fev. 13 ] -
Vancouver
Vidsiunas EK, Farah CS, Reinach F de C. Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin. Programa e resumos. 2001 ;[citado 2026 fev. 13 ] - Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity
- Regulatory properties of the 'N''H IND.2' and 'COOH' terminal domains of troponin T: ATPase activation and binding to TnI and TnC
- Fluorescence and regulatory properties of reconbinant tropomyosins containing 5-hydroxytryptophan: `Ca POT.2+'-binding to troponin results in conformational change in region of tropomyosin well away from the troponin binding site
- Structural and functional studies on troponin C interactions
- Study of `Ca POT 2+´-independent interaction of TnT with tropomyosin using a tropomyosin with a intrinsic fluorescent 5-hydroxytryotophan probe
- Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan
- Regulatory properties of recombinant tropomyosins containing 5-hydroxytryptophan: ´Ca POT. 2+´-binding to troponin results in a conformational change in a region of tropomyosin outside the troponin binding site
- Looking at 'Ca POT.2+' binding properties of troponin-C, Troponin and thin filaments using the fluorescence of a 5-OH-tryptophan probe incorporated into troponin-C
- Complete sequence of human fast-type and slow-type muscle myosin -binding-protein c (mybp-c)
- Xanthomonas genes associated with plant pathogenicity
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