Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Mikhail I. Khoroshev"'
Publikováno v:
Archives of Biochemistry and Biophysics. 402:243-248
In pioneering studies on the 31P NMR spectra of MgADP bound to the "molecular motor" myosin subfragment 1 (S1) in the temperature range of 0 to 25 degrees C, Shriver and Sykes [Biochemistry 20 (1981) 2004-2012/6357-6362; Biochemistry 21 (1982) 3022-3
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1478:138-151
Effects of subtilisin cleavage of actin between residues 47 and 48 on the conformation of F-actin and on its changes occurring upon binding of myosin subfragment-1 (S1) were investigated by measuring polarized fluorescence from rhodamine-phalloidin-
Publikováno v:
Archives of Biochemistry and Biophysics. 361:94-100
Chicken brush border myosin I has up to six IQ sequence motifs at which it may bind calmodulin. To determine the relative contributions of these motifs to calmodulin binding, fusion deletion fragments were expressed in Escherichia coli and their abil
Autor:
Mikhail I. Khoroshev, Donald B. Bivin
Publikováno v:
Journal of Photochemistry and Photobiology A: Chemistry. 78:209-214
Fluorescence decay measurements were made on six tryptophan-containing diketopiperazines (cyclo(- l -Trp- l -His-), cyclo(- l -Trp-D-His-), cyclo(- l -Trp- l -Asp-), cyclo((- l -Trp- l -Glu-) and cylo(- l -Trp- d -Glu-); Trp, tryptophan; His, histidi
Publikováno v:
FEBS Letters. 281:51-54
The effect of troponin I and caldesmon on phalloidin-rhodamine- and 1,5-IAEDANS-labelled actin in skeletal muscle ghost fibers was investigated by polarized fluorescence. Both these proteins inhibited the structural alterations in the actin monomer a
Autor:
Hugo M. Martinez, Manuel F. Morales, Kathleen Ue, Bruce D. Ray, Mikhail I. Khoroshev, Kunihiko Konno
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 97(4)
This paper describes the placement of a crosslinking agent (dibromobimane) between two thiols (Cys-522 and Cys-707) of a fragment, “S1,” of the motor protein, myosin. It turns out that fastening the first anchor of the crosslinker is easy and rap
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America. 91(18)
Many and diverse modifications of the myosin subfragment 1 (S-1) increase (modulate) its ATPase activity, including interaction of this particle with actin; a recent addition to these modifications is the extensive lysine modification of S-1 that see