Interfacial water structure controls protein conformation (Articolo in rivista)

Type
Label
  • Interfacial water structure controls protein conformation (Articolo in rivista) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/jp066206p (literal)
Alternative label
  • Der A ; Kelemen L ; Fabian L; Taneva SG ; Fodor E ; Pali T ; Cupane A ; Cacace MG ; Ramsden JJ (2008)
    Interfacial water structure controls protein conformation
    in The journal of physical chemistry. B; American Chemical Society, Washington (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Der A ; Kelemen L ; Fabian L; Taneva SG ; Fodor E ; Pali T ; Cupane A ; Cacace MG ; Ramsden JJ (literal)
Pagina inizio
  • 5344 (literal)
Pagina fine
  • 5350 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 111 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 19 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. Hungarian Acad Sci, Biol Res Ctr, Inst Biophys, H-6701 Szeged, Hungary 2. Bulgarian Acad Sci, Inst Biophys, BU-1113 Sofia, Bulgaria 3. Univ Palermo, Dept Phys & Astron Sci, I-90123 Palermo, Italy 4. INFM, I-90123 Palermo, Italy 5. CNR, ISMN, I-40129 Bologna, Italy 6. Cranfield Univ, Dept Mat, Cranfield MK43 0AL, Beds, England (literal)
Titolo
  • Interfacial water structure controls protein conformation (literal)
Abstract
  • A phenomenological theory of salt-induced Hofmeister phenomena is presented, based on a relation between protein solubility in salt solutions and protein-water interfacial tension. As a generalization of previous treatments, it implies that both kosmotropic salting out and chaotropic salting in are manifested via salt-induced changes of the hydrophobic/hydrophilic properties of protein-water interfaces. The theory is applied to describe the salt-dependent free energy profiles of proteins as a function of their water-exposed surface area. On this basis, three classes of protein conformations have been distinguished, and their existence experimentally demonstrated using the examples of bacteriorhodopsin and myoglobin. The experimental results support the ability of the new formalism to account for the diverse manifestations of salt effects on protein conformation, dynamics, and stability, and to resolve the puzzle of chaotropes stabilizing certain proteins (and other anomalies). It is also shown that the relation between interfacial tension and protein structural stability is straightforwardly linked to protein conformational fluctuations, providing a keystone for the microscopic interpretation of Hofmeister effects. Implications of the results concerning the use of Hofmeister effects in the experimental study of protein function are discussed. (literal)
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