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Protein flexibility in psychrophilic and mesophilic trypsins. Evidence of evolutionary conservation of protein dynamics in trypsin‐like serine‐proteases
Author(s) -
Papaleo Elena,
Pasi Marco,
Riccardi Laura,
Sambi Ilaria,
Fantucci Piercarlo,
Gioia Luca De
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.02.048
Subject(s) - psychrophile , proteases , serine protease , serine , flexibility (engineering) , mesophile , protease , biochemistry , biology , chemistry , enzyme , genetics , bacteria , statistics , mathematics
Psychrophilic trypsins present fewer interdomain interactions and enhanced localized flexibility in regions close to the catalytic site. Notably, these regions fit well with the pattern of protein flexibility previously reported for psychrophilic elastases. Our results indicate that specific sites within the serine‐protease fold can be considered hot spots of cold‐adaptation and that psychrophilic trypsins and elastases have independently discovered similar molecular strategies to optimize flexibility at low temperatures.