Hydrophobic interactions between the secondary structures on the molecular surface reinforce the alkaline stability of serine protease

Biotechnology Letters

Volumn 28, Issue 17, 2006, Pages 1383-1391

  Oguchi, Yuki ^a   Maeda, Hiroshi ^a   Abe, Keietsu ^a   Nakajima, Tasuku ^a   Uchida, Takafumi ^a   Yamagata, Youhei ^a  

^a TOHOKU UNIVERSITY   (Japan)

Author keywords

Alkaline stability; Hydrophobic interaction; Protein structure; Secondary structures; Subtilisin

Indexed keywords

ALKALINE STABILITY; HYDROPHOBIC INTERACTION; PROTEIN STRUCTURE; SECONDARY STRUCTURES; SUBTILISIN;

HYDROPHOBICITY; MOLECULAR DYNAMICS; PROTEINS; THERMODYNAMIC STABILITY;

MUTAGENESIS;

SERINE PROTEINASE;

ARTICLE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME STABILITY; HEAT; HYDROPHOBICITY; MUTATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

ENZYME STABILITY; HEAT; HOT TEMPERATURE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; HYDROPHOBICITY; MODELS, MOLECULAR; MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SERINE ENDOPEPTIDASES;

EID: 33747350839     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-006-9100-0     Document Type: Article

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