Showing papers by "Oliviero Carugo published in 2020"

Mobility of water and of protein atoms at the protein-water interface, monitored by anisotropic atomic displacement parameters, are largely uncorrelated

Abstract: A non-redundant set of 231 protein crystal structures refined at a resolution better than (or equal to) 1 A was extracted from the Protein Data Bank and the degree of conformational rigidity at the protein-water interface was examined by means of the Hirshfeld test and by comparing the orientations of the anisotropic Us for contacting protein and water atoms. Contacts between protein and water atoms are more rigid that contacts between water atoms and the degree of rigidity increases for shorter contacts and for more hydrogen-bonded atoms. Nevertheless, water and protein atoms are not rigidly held together. On the contrary, they seem to have little influence on their mobility to such an extent that hydration water, different from the protein atoms, cannot be considered to be properly in the solid state

Lithium-Protein Interactions: Analysis of Lithium-Containing Protein Crystal Structures Deposited in the Protein Data Bank.

Abstract: Background Despite the fact that lithium is not a biologically essential metallic element, its pharmacological properties are well known and human exposure to lithium is increasingly possible because of its used in aerospace industry and in batteries Objective: Lithium-protein interactions are therefore interesting and the surveys of the structures of lithium-protein complexes is described in this paper. Method A high quality non-redundant set of lithium containing protein crystal structures was extracted from the Protein Data Bank and the stereochemistry of the lithium first coordination sphere was examined in detail. Result Four main observations were reported: (i) lithium interacts preferably with oxygen atoms; (ii) preferably with side-chain atoms; (iii) preferably with Asp or Glu carboxylates; (iv) the coordination number tends to be four with stereochemical parameters similar to those observed in small molecules containing lithium Conclusion: Although structural information on lithium-protein, available from the Protein Data Bank, is relatively scarce, these trends appears to be so clear that one may suppose that they will be confirmed by further data that will join the Protein Data Bank in the future.