Abstract

1. Analysis of actin structure will continue using new F-actin-phalloidin data accumulated at Heidelberg. 2. Acto-S1 studies will continue: Various stiochometries of S1 to deuterated actin will be studied in order to investigate the small differences presently observed between bound and free S1. Modelling studies of these data will be initiated.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Program Projects (P01)
Project #
5P01HL016683-13
Application #
3097568
Study Section
Heart, Lung, and Blood Research Review Committee A (HLBA)
Project Start
1979-05-01
Project End
1989-04-30
Budget Start
1987-05-01
Budget End
1988-04-30
Support Year
13
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
University of California San Francisco
Department
Type
Schools of Medicine
DUNS #
073133571
City
San Francisco
State
CA
Country
United States
Zip Code
94143

  Publications

Muhlrad, A (1991) The isolated 21 kDa N-terminal fragment of myosin binds to actin in an ATP and ionic strength-dependent manner. Biochim Biophys Acta 1077:308-15
Curmi, P M; Stone, D B; Schneider, D K et al. (1991) Mechanism of force generation studied by neutron scattering. Adv Biophys 27:131-42
Mendelson, R A; Bivin, D; Curmi, P M et al. (1991) Recent neutron scattering studies of muscle contraction and its control. Adv Biophys 27:143-53
Muhlrad, A; Chaussepied, N (1990) Effect of nucleotides, actin and temperature on thermolysin digestion of myosin subfragment-1. Eur J Biochem 192:663-8
Muhlrad, A (1989) Isolation and characterization of the N-terminal 23-kilodalton fragment of myosin subfragment 1. Biochemistry 28:4002-10
Botts, J; Thomason, J F; Morales, M F (1989) On the origin and transmission of force in actomyosin subfragment 1. Proc Natl Acad Sci U S A 86:2204-8
Kasprzak, A A; Chaussepied, P; Morales, M F (1989) Location of a contact site between actin and myosin in the three-dimensional structure of the acto-S1 complex. Biochemistry 28:9230-8
Chaussepied, P (1989) Interaction between stretch of residues 633-642 (actin binding site) and nucleotide binding site on skeletal myosin subfragment 1 heavy chain. Biochemistry 28:9123-8
Miyanishi, T; Borejdo, J (1989) Differential behavior of two cysteine residues on the myosin head in muscle fibers. Biochemistry 28:1287-94
Chaussepied, P; Kasprzak, A A (1989) Change in the actin-myosin subfragment 1 interaction during actin polymerization. J Biol Chem 264:20752-9

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