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NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G.
Gouda H, Shiraishi M, Takahashi H, Kato K, Torigoe H, Arata Y, Shimada I. Gouda H, et al. Among authors: arata y. Biochemistry. 1998 Jan 6;37(1):129-36. doi: 10.1021/bi970923f. Biochemistry. 1998. PMID: 9425032
A previous NMR analysis has shown that in solution FB is composed of a bundle of three alpha-helices, helix I, helix II, and helix III [Gouda, H., Torigoe, H., Saito, A., Sato, M., Arata, Y., and Shimada, I. (1992) Biochemistry 31, 9665-9672]. In contrast, the cryst …
A previous NMR analysis has shown that in solution FB is composed of a bundle of three alpha-helices, helix I, helix II, and helix III [Goud …
A multinuclear NMR study of the active site of an endoglucanase from a strain of Bacillus. Use of Trp residues as structural probes.
Kawaminami S, Takahashi H, Ito S, Arata Y, Shimada I. Kawaminami S, et al. Among authors: arata y. J Biol Chem. 1999 Jul 9;274(28):19823-8. doi: 10.1074/jbc.274.28.19823. J Biol Chem. 1999. PMID: 10391926 Free article.
In the hydrolytic reaction catalyzed by an endoglucanase from a Bacillus strain (endoglucanase K), 2 of 12 Trp residues, Trp174 and Trp243, are responsible for binding of the substrate and/or for the catalysis (Kawaminami, S., Ozaki, K., Sumitomo, N., Hayashi, Y., Ito, S., …
In the hydrolytic reaction catalyzed by an endoglucanase from a Bacillus strain (endoglucanase K), 2 of 12 Trp residues, Trp174 and Trp243, …
300 results