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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":243507,"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. Bacteriol. 187(17): 6206-6212. dx.doi.org/10.1128/JB.187.17.6206-6212.2005","AutID":243507,"MonDate":null,"AnaDate":2005,"PeerRev":1,"outputType":"1_A1","OpenAcc":0},{"BRefID":281063,"RR":"D'Amico, S.; Claverie, P.; Collins, T.; Georlette, D.; Gratia, E.; Hoyoux, A.; Meuwis, M.-A.; Feller, G.; Gerday, C. (2002). Molecular basis of cold adaptation. Phil. Trans. R. Soc. Lond. (B Biol. 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