Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms(353 views) Balasco N, Esposito L, De Simone A, Vitagliano L
Protein Sci (ISSN: 0961-8368, 1469-896xelectronic), 2013 Jul; 22(7): 1016-1023.
Keywords: B-Hairpins, Data Mining, Loop Shortening, Protein Stability, Protein Structure And Stability, Ribonuclease A, Thioredoxin, Article, Mesophile, Nonhuman, Priority Journal, Protein Conformation, Protein Isolation, Protein Motif, Protein Secondary Structure, Thermophile, Thermostability, Amino Acid Sequence, Bacterium, Chemistry, Molecular Genetics, Protein Database, Sequence Alignment, Sequence Analysis, Statistical Model, Molecular Sequence Data,
Affiliations: *** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Via Mezzocannone 16, Napoli I-80134, Italy
Dipartimento di Scienze e Tecnologie Ambientali Biologiche e Farmaceutiche, Seconda Universita di Napoli, Caserta 81100, Italy
Division of Molecular Biosciences, Imperial College London, London SW7 2AZ, United Kingdom
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Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms
It has been recently discovered that the connection of secondary structure elements (-unit, - and -units) in proteins follows quite stringent principles regarding the chirality and the orientation of the structural units (Koga et al., Nature 2012;491:222-227). By exploiting these rules, a number of protein scaffolds endowed with a remarkable thermal stability have been designed (Koga et al., Nature 2012;491:222-227). By using structural databases of proteins isolated from either mesophilic or thermophilic organisms, we here investigate the influence of supersecondary associations on the thermal stability of natural proteins. Our results suggest that -hairpins of proteins from thermophilic organisms are very frequently characterized by shortenings of the loops. Interestingly, this shortening leads to states that display a very strong preference for the most common connectivity of the strands observed in native protein hairpins. The abundance of selective states in these proteins suggests that they may achieve a high stability by adopting a strategy aimed to reduce the possible conformations of the unfolded ensemble. In this scenario, our data indicate that the shortening is effective if it increases the adherence to these rules. We also show that this mechanism may operate in the stabilization of well-known protein folds (thioredoxin and RNase A). These findings suggest that future investigations aimed at defining mechanism of protein stabilization should also consider these effects.
Role of loops connecting secondary structure elements in the stabilization of proteins isolated from thermophilic organisms
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(449 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote