Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
HYDROPHOBIC REGIONS ON PROTEIN SURFACES - DEFINITION BASED ON HYDRATION SHELL STRUCTURE AND A QUICK METHOD FOR THEIR COMPUTATION
Autore:
EISENHABER F; ARGOS P;
Indirizzi:
HUMBOLDT UNIV BERLIN,INST BIOCHEM CHARITE,FAK MED,HESS STR 3-4 D-10098 BERLIN GERMANY EUROPEAN MOL BIOL LAB D-69012 HEIDELBERG GERMANY
Titolo Testata:
Protein engineering
fascicolo: 12, volume: 9, anno: 1996,
pagine: 1121 - 1133
SICI:
0269-2139(1996)9:12<1121:HROPS->2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC TRYPSIN-INHIBITOR; MAGNETIC-RESONANCE; WATER-MOLECULES; RESIDENCE TIMES; FREE-ENERGY; GLOBULAR-PROTEINS; POLAR-SOLVENTS; BURIED WATER; BOUND WATER; DATA-BANK;
Keywords:
CONFORMATIONAL ENERGY; HYDROPHOBIC EFFECT; HYDROPHOBIC SURFACE REGION; MOLECULAR RECOGNITION; SOLVENT-ACCESSIBLE SURFACE OF PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
82
Recensione:
Indirizzi per estratti:
Citazione:
F. Eisenhaber e P. Argos, "HYDROPHOBIC REGIONS ON PROTEIN SURFACES - DEFINITION BASED ON HYDRATION SHELL STRUCTURE AND A QUICK METHOD FOR THEIR COMPUTATION", Protein engineering, 9(12), 1996, pp. 1121-1133

Abstract

The hydrophobic part of the solvent-accessible surface of a typical monomeric globular protein consists of a single, large interconnected region formed from faces of apolar atoms and constituting similar to 60% of the solvent-accessible surface area, Therefore, the direct delineation of the hydrophobic surface patches on an atom-wise basis is impossible. Experimental data indicate that, in a two-state hydration model, a protein can be considered to be unified with its first hydration shell in its interaction with bulk water, We show that, if the surfacearea occupied by water molecules bound at polar protein atoms as generated by AUTOSOL is removed, only about two-thirds of the hydrophobic part of the protein surface remains accessible to bulk solvent. Moreover, the organization of the hydrophobic part of the solvent-accessiblesurface experiences a drastic change, such that the single interconnected hydrophobic region disintegrates into many smaller patches, i.e. the physical definition of a hydrophobic surface region as unoccupied by first hydration shell water molecules can distinguish between hydrophobic surface clusters and small interconnecting channels, It is these remaining hydrophobic surface pieces that probably play an importantrole in intra- and intermolecular recognition processes such as ligand binding, protein folding and protein-protein association in solutionconditions, These observations have led to the development of an accurate and quick analytical technique for the automatic determination ofhydrophobic surface patches of proteins, This technique is not aggravated by the limiting assumptions of the methods for generating explicit water hydration positions, Formation of the hydrophobic surface regions owing to the structure of the first hydration shell can be computationally simulated by a small radial increment in solvent-accessible polar atoms, followed by calculation of the remaining exposed hydrophobic patches, We demonstrate that a radial increase of 0.35-0.50 Angstrom resembles the effect of tightly bound water on the organization of the hydrophobic part of the solvent-accessible surface.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 17:52:34