Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin (2003)
- Authors:
- USP affiliated authors: MIRANDA, MARIA TERESA MACHINI DE - IQ ; FARAH, SHAKER CHUCK - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher: Biophysical Society Office
- Publisher place: Bethesda
- Date published: 2003
- Source:
- Título do periódico: Biophysical Journal
- ISSN: 0006-3495
- Volume/Número/Paginação/Ano: v. 84, n. 2, res. 1211-Pos, 2003
- Conference titles: Annual Meeting of the Biophysical Society
-
ABNT
PAULUCCI, Adriana Aparecida; HICKS, Leslie; MACHADO, Alessandra; et al. Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin. Biophysical Journal[S.l: s.n.], 2003. -
APA
Paulucci, A. A., Hicks, L., Machado, A., Miranda, M. T. M. de, Kay, C. M., & Farah, C. S. (2003). Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin. Biophysical Journal. Bethesda: Biophysical Society Office. -
NLM
Paulucci AA, Hicks L, Machado A, Miranda MTM de, Kay CM, Farah CS. Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin. Biophysical Journal. 2003 ; 84( 2): -
Vancouver
Paulucci AA, Hicks L, Machado A, Miranda MTM de, Kay CM, Farah CS. Specific sequences determine the stability and cooperativity of folding of the C-terminal half of tropomyosin. Biophysical Journal. 2003 ; 84( 2): - Stability studies of tropomyosin fragments and its interaction with troponin
- Stability studies of tropomyosin fragments
- Stability of troponin I and T investigated by a hydrophobic fluorescent probe
- Calcium binding to Leptospira outer membrane antigen LipL32 is not necessary for its interaction with plasma fibronectin, collagen type IV, and plasminogen
- Ca2+-induced rolling of tropomyosin in muscle thin filaments - The alpha- and beta-band hypothesis revisited
- High-throughput screening of Xanthomonas axonopodis pv citri targets for structural proteomics using NMR
- Deciphering the head-to-tail complex of 'alpha'-tropomyosin using double mutant cycles and molecular docking
- Analyses of protein-protein interactions involving Xanthomonas axonopodis pv citri RNA polimerase sigma factors
- Strategy for determining the binding site of tropomyosin on actin
- A tropomyosin mutant containing a intrinsic fluorescent probe may be used to study head-to-tail interaction thermodynamics
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