title: An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius.
abstract: We report a crystallographic and computational analysis of two mutant forms of the Alicyclobacillus acidocaldarius thioredoxin (BacTrx) done in order to evaluate the contribution of two specific amino acids to the thermostability of BacTrx. Our results suggest that the thermostability of BacTrx may be modulated by mutations affecting the overall electrostatic energy of the protein.
authors.affiliation: Dipartimento di Chimica Biologica, University of Naples Federico II, Istituto di Biostrutture e Bioimmagini-CNR, 80134 Naples, Italy.
authors.forename: Simonetta
authors.initials: S
authors.lastname: Bartolucci
authors.forename: Giuseppina
authors.initials: G
authors.lastname: De Simone
authors.forename: Stefania
authors.initials: S
authors.lastname: Galdiero
authors.forename: Roberto
authors.initials: R
authors.lastname: Improta
authors.forename: Valeria
authors.initials: V
authors.lastname: Menchise
authors.forename: Carlo
authors.initials: C
authors.lastname: Pedone
authors.forename: Emilia
authors.initials: E
authors.lastname: Pedone
authors.forename: Michele
authors.initials: M
authors.lastname: Saviano
mesh_terms: D001407:Bacillus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D019295:Computational Biology / Q000379:methods*; D003460:Crystallization; D018360:Crystallography, X-Ray; D006358:Hot Temperature; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009154:Mutation; D011487:Protein Conformation; D017510:Protein Folding; D013329:Structure-Activity Relationship; D013879:Thioredoxins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
chemical_list: D013879:Thioredoxins