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Role of lysine versus arginine in enzyme cold-adaptation: modifying lysine to homo-arginine stabilizes the cold-adapted α-amylase from Pseudoalteramonas haloplanktis. Proteins-Structure Function and Bioinformatics 64(2): 486-501. https://dx.doi.org/10.1002/prot.20989","AutID":242496,"MonDate":null,"AnaDate":2006,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280927,"RR":"Siddiqui, K.S.; Feller, G.; D'Amico, S.; Gerday, C.; Giaquinto, L.; Cavicchioli, R. (2005). The active site is the least stable structure in the unfolding pathway of a multidomain cold-adapted α-amylase. J. Bacteriol. 187(17): 6197-6205. dx.doi.org/10.1128/JB.187.17.6197-6205.2005","AutID":242496,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":280928,"RR":"Siddiqui, K.S.; Poljak, A.; Guilhaus, M.; Feller, G.; D'Amico, S.; Gerday, C.; Cavicchioli, R. (2005). Role of disulfide bridges in the activity and stability of a cold-active α-amylase. J. 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