Thermostabilization by replacement of specific residues with lysine in a Bacillus alkaline cellulase: Building a structural model and implications of newly formed double intrahelical salt bridges

Protein Engineering

Volumn 14, Issue 7, 2001, Pages 501-504

  Ozawa, Tadahiro ^a   Hakamada, Yoshihiro ^a   Hatada, Yuji ^a   Kobayashi, Tohru ^a   Shirai, Tsuyoshi ^b   Ito, Susumu ^a  

^a KAO CORPORATION   (Japan)

^b NAGOYA UNIVERSITY   (Japan)

Author keywords

Bacillus; Cellulase; Intrahelix; Ion pair; Salt bridge; Thermostability

Indexed keywords

ASPARAGINE; ASPARTIC ACID; BETA GLUCAN HYDROLASE; CARBONYL DERIVATIVE; CELLULASE; GLUTAMIC ACID; HYDROGEN; ION; LYSINE; MUTANT PROTEIN; OXYGEN; SERINE;

ALKALINITY; ALPHA HELIX; AMINO ACID SUBSTITUTION; ARTICLE; BACILLUS; CHEMICAL BOND; CONTROLLED STUDY; ENZYME STRUCTURE; MODEL; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS; THERMOSTABILITY;

BACILLUS SP.; BACTERIA (MICROORGANISMS);

EID: 0034857949     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: 10.1093/protein/14.7.501     Document Type: Article

References (43)