Recognition and Stabilization of A Unique CPRI—Structural Motif in Cucurbitaceae Family Trypsin Inhibitor Peptides: Molecular Dynamics Based Homology Modeling Using the X-ray Structure of MCTI-II
Author:
Affiliation:
1. a Department of Biophysics , Bose Institute , P1/12, C.I.T. Scheme VII M, Calcutta , 700054 , India
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
https://www.tandfonline.com/doi/pdf/10.1080/07391102.2001.10506689
Reference18 articles.
1. 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
2. The interpretation of protein structures: Estimation of static accessibility
3. Structure and energetics of ligand binding to proteins:Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system
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1. Plant Serine Proteinase Inhibitors;Protein & Peptide Letters;2005-07-01
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