Natural abundance 15 N NMR assignments delineate structural differences between intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor III
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80607-I/fullpdf
Reference20 articles.
1. The squash family of serine proteinase inhibitors. Amino acid sequences and association equilibrium constants of inhibitors from squash, summer squash, zucchini, and cucumber seeds
2. Inhibition of Serine Proteinases by Squash Inhibitors
3. The refined 2.0 Å X-ray crystal structure of the complex formed between bovine β-trypsin and CMTI-I, a trypsin inhibitor from squash seeds (Cucurbita maxima) Topological similarity of the squash seed inhibitors with the carboxypeptidase A inhibitor from p
4. Determination of the complete three-dimensional structure of the trypsin inhibitor from squash seeds in aqueous solution by nuclear magnetic resonance and a combination of distance geometry and dynamical simulated annealing
5. Pumpkin seed inhibitor of human factor XIIa (activated Hageman factor) and bovine trypsin
Cited by 3 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Plant Serine Proteinase Inhibitors;Protein & Peptide Letters;2005-07-01
2. 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;Protein Science;1998-01
3. Chemical Synthesis, Molecular Cloning, Overexpression, and Site-Directed Mutagenesis of the Gene Coding for Pumpkin (Curcubita maxima) Trypsin Inhibitor CMTI-V;Protein Expression and Purification;1993-06
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