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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: gong y. 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]. ...
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., …
NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.
Liu J, Gong Y, Prakash O, Wen L, Lee I, Huang JK, Krishnamoorthi R. Liu J, et al. Among authors: gong y. Protein Sci. 1998 Jan;7(1):132-41. doi: 10.1002/pro.5560070114. Protein Sci. 1998. PMID: 9514268 Free PMC article.
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