Core - Biophysical and Biochemical Facilities

Abstract

Core B provides technical support for all projects. It includes three parts: (1) Protein Chemistry: provides amino acid composition and sequence analyses, and synthesis of peptides using various state-of-the-art facilities. It will also offer advice to individual PI's on peptide/fragment purification and characterization. This service will be used essentially by every project, with less emphasis in Projects II-C and III. (2) Analytical Ultracentrifugation: provides both sedimentation velocity and sedimentation equilibrium runs, as well as related hydrodynamic analyses; it will support Projects I-A, I-B, II-A and II-B. (3) Electron Microscopy and Immunocytochemistry: provides technical expertise and advice for the EM visualization of proteins, especially with an improved rotary shadowing technique recently developed by one of the PI's, and supports the preparation of polyclonal and monoclonal antibodies, including the handling of laboratory animals. This service will be needed in Projects I-A, II-A, II-B and possibly I-B and III.

Funding Agency

• Agency: National Institute of Health (NIH)
• Institute: National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS)
• Type: Research Program Projects (P01)
• Project #: 5P01AR041637-05
• Application #: 2336234
• Budget Start: 1995-10-01
• Budget End: 1996-09-30
• Support Year: 5
• Fiscal Year: 1996

Institution

• Name: Boston Biomedical Research Institute
• DUNS #: 058893371
• City: Watertown
• State: MA
• Country: United States
• Zip Code: 02472

Publications

Guo, Hongqiu; Huang, Renjian; Semba, Shingo et al. (2013) Ablation of smooth muscle caldesmon affects the relaxation kinetics of arterial muscle. Pflugers Arch 465:283-94

Mabuchi, Yasuko; Mabuchi, Katsuhide; Stafford, Walter F et al. (2010) Modular structure of smooth muscle Myosin light chain kinase: hydrodynamic modeling and functional implications. Biochemistry 49:2903-17

Gali?ska, Agnieszka; Hatch, Victoria; Craig, Roger et al. (2010) The C terminus of cardiac troponin I stabilizes the Ca2+-activated state of tropomyosin on actin filaments. Circ Res 106:705-11

Hayes, David; Napoli, Vanessa; Mazurkie, Andrew et al. (2009) Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function. J Biol Chem 284:18801-7

Mudalige, Wasana A K A; Tao, Terence C; Lehrer, Sherwin S (2009) Ca2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the C-terminal domain of troponin I in reconstituted skeletal muscle thin filaments. J Mol Biol 389:575-83

Greenberg, M J; Wang, C-L A; Lehman, W et al. (2008) Modulation of actin mechanics by caldesmon and tropomyosin. Cell Motil Cytoskeleton 65:156-64

Coulton, Arthur T; Koka, Kezia; Lehrer, Sherwin S et al. (2008) Role of the head-to-tail overlap region in smooth and skeletal muscle beta-tropomyosin. Biochemistry 47:388-97

Sumida, John P; Wu, Eleanor; Lehrer, Sherwin S (2008) Conserved Asp-137 imparts flexibility to tropomyosin and affects function. J Biol Chem 283:6728-34

Wang, C L Albert (2008) Caldesmon and the regulation of cytoskeletal functions. Adv Exp Med Biol 644:250-72

Lee, Eunhee; Hayes, David B; Langsetmo, Knut et al. (2007) Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase. J Mol Biol 373:1198-212