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Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties
BACKGROUND: EstE1 is a hyperthermophilic esterase belonging to the hormone-sensitive lipase family and was originally isolated by functional screening of a metagenomic library constructed from a thermal environmental sample. Dimers and oligomers may have been evolutionally selected in thermophiles b...
Autores principales: | Byun, Jung-Sue, Rhee, Jin-Kyu, Kim, Nam Doo, Yoon, JeongHyeok, Kim, Dong-Uk, Koh, Eunhee, Oh, Jong-Won, Cho, Hyun-Soo |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2007
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1936996/ https://www.ncbi.nlm.nih.gov/pubmed/17625021 http://dx.doi.org/10.1186/1472-6807-7-47 |
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