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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: krishnamoorthi r. 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 backbone dynamics of uniformly 15N-labeled rCMTI-V were characterized by 2D …
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., & Krish …
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. Among authors: krishnamoorthi r. 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 consequences of these hydrogen-bondi …
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. …
Internal mobility of reactive-site-hydrolyzed recombinant Cucurbita maxima trypsin inhibitor-V characterized by NMR spectroscopy: evidence for differential stabilization of newly formed C- and N-termini.
Liu J, Prakash O, Huang Y, Wen L, Wen JJ, Huang JK, Krishnamoorthi R. Liu J, et al. Among authors: krishnamoorthi r. Biochemistry. 1996 Sep 24;35(38):12503-10. doi: 10.1021/bi9609329. Biochemistry. 1996. PMID: 8823186
The 1H-15N chemical shift correlation spectra of rCMTI-V* were assigned, and the chemical shift data were compared with those available for rCMTI-V [Liu, J., Prakash, O., Cai, M., Gong, Y., Huang, Y., Wen, L., Wen, J. J., Huang, J.-K., & Krishnamoorthi, R. (1996 …
The 1H-15N chemical shift correlation spectra of rCMTI-V* were assigned, and the chemical shift data were compared with those available for …
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: krishnamoorthi r. Protein Sci. 1998 Jan;7(1):132-41. doi: 10.1002/pro.5560070114. Protein Sci. 1998. PMID: 9514268 Free PMC article.
118 results