Zobrazeno 1 - 10
of 124
pro vyhledávání: '"John Gergely"'
Autor:
Jeremy McMinis, David M. Ceperley, Jeongnim Kim, John Gergely, Jeffrey M. McMahon, Miguel A. Morales
Publikováno v:
Journal of chemical theory and computation. 10(6)
The accurate description of the thermodynamic and dynamical properties of liquid water from first-principles is a very important challenge to the theoretical community. This represents not only a critical test of the predictive capabilities of first-
Autor:
John Gergely
Publikováno v:
Journal of Muscle Research and Cell Motility. 27:215-220
Autor:
John Gergely, Sumiko Kimura
Publikováno v:
Journal of Muscle Research and Cell Motility. 26:277-284
Publikováno v:
Biochemistry. 41:12891-12898
We reported previously that both residues 48 and 82 on opposite sides of troponin-C's (TnC's) N-terminal regulatory hydrophobic cleft photo-cross-linked to Met 121 of troponin-I (TnI) [Luo, Y., Leszyk, J., Qian, Y., Gergely, J., and Tao, T. (1999) Bi
Publikováno v:
Journal of Molecular Biology. 316:429-434
Striated muscles are regulated by Ca 2+ via the thin filament proteins troponin (Tn) and tropomyosin (Tm). In the absence of Ca 2+ , contraction is inhibited, whereas myosin-actin interaction and contraction can take place in its presence. Although i
Publikováno v:
Biochemistry. 39:15306-15315
Skeletal muscle troponin C (TnC) adopts an extended conformation when crystallized alone and a compact one when crystallized with an N-terminal troponin I (TnI) peptide, TnI(1-47) [Vassylyev et al. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852].
Publikováno v:
Journal of Molecular Biology. 296:899-910
The interaction sites of rabbit skeletal troponin I (TnI) with troponin C (TnC), troponin T (TnT), tropomyosin (Tm) and actin were mapped systematically using nine single cysteine residue TnI mutants with mutation sites at positions 6, 48, 64, 89, 10
Publikováno v:
Biochemistry. 38:6678-6688
It has been proposed [Herzberg et al. (1986) J. Biol. Chem. 261, 2638-2644], and confirmed by structural studies [Gagne et al. (1995) Nat. Struct. Biol. 2, 784-789], that the binding of Ca2+ to the triggering sites in troponin-C (TnC) causes the open
Publikováno v:
Journal of Muscle Research and Cell Motility. 19:479-490
Our previous studies have shown that 4-maleimidobenzophenone (BP-Mal) attached to troponin-C (TnC) mutants with single cysteines at positions 12, 57, 89 and 98 forms crosslinks to troponin-I (TnI), and the identified crosslinking regions indicate an
Publikováno v:
Biochemistry. 36:11027-11035
Contraction of vertebrate striated muscle is regulated by the interaction of Ca2+ with the heterotrimeric protein troponin (Tn), composed of troponin-C (TnC), troponin-I (TnI), and troponin-T (TnT). Although much is known about the Ca2+-induced confo