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 (1999)
- Authors:
- USP affiliated authors: FARAH, SHAKER CHUCK - IQ ; REINACH, FERNANDO DE CASTRO - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; ESCHERICHIA COLI
- Language: Inglês
- Imprenta:
- Publisher place: Washington
- Date published: 1999
- Source:
- Título do periódico: Biochemistry
- ISSN: 0006-2960
- Volume/Número/Paginação/Ano: v. 38, n. 32, p. 10543-10551, 1999
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ABNT
FARAH, Chuck Shaker e REINACH, Fernando de Castro. 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. Biochemistry, v. 38, n. 32, p. 10543-10551, 1999Tradução . . Acesso em: 25 abr. 2024. -
APA
Farah, C. S., & Reinach, F. de C. (1999). 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. Biochemistry, 38( 32), 10543-10551. -
NLM
Farah CS, Reinach F de C. 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. Biochemistry. 1999 ; 38( 32): 10543-10551.[citado 2024 abr. 25 ] -
Vancouver
Farah CS, Reinach F de C. 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. Biochemistry. 1999 ; 38( 32): 10543-10551.[citado 2024 abr. 25 ] - 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
- Purification of 10 tropomyosin mutants for mapping the interface between tropomyosin and actin
- Mapping the domain in troponin T responsible for the activation of actomyosin ATPase activity
- Fluorescence properties of recombinant tropomyosin containing tryptophan, 5-hydroxytryptophan and 7-azatryptophan
- 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
- Regulatory properties of the 'N''H IND.2' and 'COOH' terminal domains of troponin T: ATPase activation and binding to TnI and TnC
- 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)
- Parallel measurement of 'Ca POT. 2+' binding and fluorescence emission upon 'Ca POT. 2+' titration of recombinant skeletal muscle troponin C - Measurement of sequential calcium binding to the regulatory sites
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