Asp30 of Aspergillus oryzae cutinase CutL1 is involved in the ionic interaction with fungal hydrophobin RolA.
Terauchi, Yuki
Asp30 of Aspergillus oryzae cutinase CutL1 is involved in the ionic interaction with fungal hydrophobin RolA. [electronic resource] - Bioscience, biotechnology, and biochemistry Jul 2017 - 1363-1368 p. digital
Publication Type: Journal Article
1347-6947
10.1080/09168451.2017.1321952 doi
Amino Acid Motifs
Aspartic Acid--chemistry
Aspergillus oryzae--chemistry
Binding Sites
Biodegradable Plastics--chemistry
Carboxylic Ester Hydrolases--chemistry
Cloning, Molecular
Escherichia coli--genetics
Fungal Proteins--chemistry
Gene Expression
Hydrophobic and Hydrophilic Interactions
Kinetics
Models, Molecular
Mutation
Polymers--chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Recombinant Proteins--chemistry
Static Electricity
Substrate Specificity
Asp30 of Aspergillus oryzae cutinase CutL1 is involved in the ionic interaction with fungal hydrophobin RolA. [electronic resource] - Bioscience, biotechnology, and biochemistry Jul 2017 - 1363-1368 p. digital
Publication Type: Journal Article
1347-6947
10.1080/09168451.2017.1321952 doi
Amino Acid Motifs
Aspartic Acid--chemistry
Aspergillus oryzae--chemistry
Binding Sites
Biodegradable Plastics--chemistry
Carboxylic Ester Hydrolases--chemistry
Cloning, Molecular
Escherichia coli--genetics
Fungal Proteins--chemistry
Gene Expression
Hydrophobic and Hydrophilic Interactions
Kinetics
Models, Molecular
Mutation
Polymers--chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Recombinant Proteins--chemistry
Static Electricity
Substrate Specificity