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Complete assignment of the aromatic proton magnetic resonance spectrum of the kringle 1 domain from human plasminogen: structure of the ligand-binding site.
Motta A, Laursen RA, Llinás M, Tulinsky A, Park CH. Motta A, et al. Among authors: llinas m. Biochemistry. 1987 Jun 30;26(13):3827-36. doi: 10.1021/bi00387a014. Biochemistry. 1987. PMID: 2820478
The Tyr ring signals were identified by reference to the recently reported spectra of the plasminogen kringle 4 homologues from human, bovine, and porcine origin [Ramesh, V., Gyenes, M., Patthy, L., & Llinas, M. (1986) Eur. J. Biochem. 159, 581-595]. ...
The Tyr ring signals were identified by reference to the recently reported spectra of the plasminogen kringle 4 homologues from human, bovin …
1H NMR studies of aliphatic ligand binding to human plasminogen kringle 4.
Petros AM, Ramesh V, Llinás M. Petros AM, et al. Among authors: llinas m. Biochemistry. 1989 Feb 7;28(3):1368-76. doi: 10.1021/bi00429a064. Biochemistry. 1989. PMID: 2496756
These results add support to a previously reported model of the kringle 4 lysine-binding site [Ramesh, V., Petros, A. M., Llinas, M., Tulinsky, A., & Park, C. H. (1987) J. Mol. Biol. 198, 481-498] by which these aromatic groups are assigned a key role in …
These results add support to a previously reported model of the kringle 4 lysine-binding site [Ramesh, V., Petros, A. M., Llinas …
324 results