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Solution structure and backbone dynamics of recombinant Cucurbita maxima trypsin inhibitor-V determined by NMR spectroscopy.
Liu J, Prakash O, Cai M, Gong Y, Huang Y, Wen L, Wen JJ, Huang JK, Krishnamoorthi R. Liu J, et al. Among authors: cai m. Biochemistry. 1996 Feb 6;35(5):1516-24. doi: 10.1021/bi952466d. Biochemistry. 1996. PMID: 8634282
The average structure of rCMTI-V is found to be almost the same as that of the native protein [Cai, M., Gong, Y., Kao, J.-L., & Krishnamoorthi, R. (1995) Biochemistry 34, 5201-5211]. ...Soc. 104, 4546-4559, 4559-4570], the following parameters were determined: o …
The average structure of rCMTI-V is found to be almost the same as that of the native protein [Cai, M., Gong, Y., Kao, J.-L., …
Differential modulation of binding loop flexibility and stability by Arg50 and Arg52 in Cucurbita maxima trypsin inhibitor-V deduced by trypsin-catalyzed hydrolysis and NMR spectroscopy.
Cai M, Huang Y, Prakash O, Wen L, Dunkelbarger SP, Huang JK, Liu J, Krishnamoorthi R. Cai M, et al. Biochemistry. 1996 Apr 16;35(15):4784-94. doi: 10.1021/bi953038a. Biochemistry. 1996. PMID: 8664268
The side chains of Arg50 and Arg52 iin Cucurbita maxima trypsin inhibitor-V (CMTI-V) anchor the binding loop to the scaffold region [Cai, M., Gong, Y., Kao, J.L-F., & Krishnamoorthi, R. (1995) Biochemistry 34, 5201-5211]. ...
The side chains of Arg50 and Arg52 iin Cucurbita maxima trypsin inhibitor-V (CMTI-V) anchor the binding loop to the scaffold region [Cai
4,681 results