Analysis of structural and physico-chemical parameters involved in the specificity of binding between α-amylases and their inhibitors

Protein Engineering

Volumn 13, Issue 3, 2000, Pages 167-177

  Da Silva, M C M ^a   Grossi De Sa M F ^a   Chrispeels, M J ^b   Togawa, R C ^a   Neshich, G ^a  

^a EMBRAPA RECURSOS GENÉTICOS E BIOTECNOLOGIA   (Brazil)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Amylase inhibitor; Charge compatibility; Hydrogen bond net; Interface forming residues; Protein interactions

Indexed keywords

AMYLASE; COMPLEMENTARY DNA; ENZYME INHIBITOR;

AMINO ACID SEQUENCE; ARTICLE; COMPLEX FORMATION; COMPUTER PROGRAM; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME INHIBITION; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; TENEBRIO;

ACANTHOSCELIDES OBTECTUS; PHASEOLUS (ANGIOSPERM); PHASEOLUS VULGARIS; SUIDAE; TENEBRIO; TENEBRIO MOLITOR; ZABROTES SUBFASCIATUS;

EID: 0034017054     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/13.3.167     Document Type: Article

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