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Cysteine mutants of light chain-2 form disulfide bonds in skeletal muscle myosin.
Wolff-Long VL, Saraswat LD, Lowey S. Wolff-Long VL, et al. Among authors: lowey s. J Biol Chem. 1993 Nov 5;268(31):23162-7. J Biol Chem. 1993. PMID: 8226834 Free article.
Multiple disulfide bonds form in recombinant myosin light chain-2 mutants that contain an engineered cysteine at positions 2, 73, or 94, in addition to the endogenous cysteines at residues 126 and 155 (Saraswat, L.D., and Lowey, S. (1991) J. Biol. Chem. 266, 1977). …
Multiple disulfide bonds form in recombinant myosin light chain-2 mutants that contain an engineered cysteine at positions 2, 73, or 94, in …
Subunit interactions within an expressed regulatory domain of chicken skeletal myosin. Location of the NH2 terminus of the regulatory light chain by fluorescence resonance energy transfer.
Saraswat LD, Lowey S. Saraswat LD, et al. Among authors: lowey s. J Biol Chem. 1998 Jul 10;273(28):17671-9. doi: 10.1074/jbc.273.28.17671. J Biol Chem. 1998. PMID: 9651364 Free article.
These fluorescence resonance energy transfer distances (24-30 A), together with a previous measurement between Cys2 and Cys155 (Wolff-Long, V. L., Tao, T., and Lowey, S. (1995) J. Biol. Chem. 270, 31111-31118) suggest a location for the NH2 terminus of RLC that appe …
These fluorescence resonance energy transfer distances (24-30 A), together with a previous measurement between Cys2 and Cys155 (Wolff-Long, …
Mapping single cysteine mutants of light chain 2 in chicken skeletal myosin.
Saraswat LD, Pastra-Landis SC, Lowey S. Saraswat LD, et al. Among authors: lowey s. J Biol Chem. 1992 Oct 15;267(29):21112-8. J Biol Chem. 1992. PMID: 1400421 Free article.
These mapping studies, together with our finding that cysteines widely separated in the primary sequence can form multiple disulfide bonds (Saraswat, L.D., and Lowey, S. (1991) J. Biol. Chem. 226, 19777-19785), support a model for LC2 as a flexible, globular molecul …
These mapping studies, together with our finding that cysteines widely separated in the primary sequence can form multiple disulfide bonds ( …
Engineered cysteine mutants of myosin light chain 2. Fluorescent analogues for structural studies.
Saraswat LD, Lowey S. Saraswat LD, et al. Among authors: lowey s. J Biol Chem. 1991 Oct 15;266(29):19777-85. J Biol Chem. 1991. PMID: 1918082 Free article.
By oxidizing the endogenous cysteines to an intramolecular disulfide bond (Katoh, T., and Lowey, S., (1989) J. Cell Biol. 109, 1549), it was expected that the new cysteine could be selectively labeled with a fluorescent probe. ...
By oxidizing the endogenous cysteines to an intramolecular disulfide bond (Katoh, T., and Lowey, S., (1989) J. Cell Biol. 109, …
112 results