In striated muscle, the thin filament consists of polymerized actin, which is decorated with the regulatory proteins troponin C (TnC) and tropomyosin. TnC is a single-polypeptide protein with a molecular weight near 18,000. We study the regulatory domain of TnC from chiken skeletal muscle using genetically generated mutants which contain a single tryptophan at positions 22, 52, and 90. The quantum yields of Trp-22 are 0.33 and 0.25 in the presence of Mg2+ (2-Mg state) and Ca2+ (4-Ca state), respectively. The anisotropy decay of of all three tryptophans show two rotational correlation times. The long correlation time observed for Trp-22 and Trp-90 suggest an asymmetric hydrodynamic shape. Data obtained at the CFS showed that TnC becomes more asymmetric upon binding the activator Ca2+.?

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR008119-06
Application #
6282891
Study Section
Project Start
1998-04-01
Project End
1999-03-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
6
Fiscal Year
1998
Total Cost
Indirect Cost
Name
University of Maryland Baltimore
Department
Type
DUNS #
003255213
City
Baltimore
State
MD
Country
United States
Zip Code
21201
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