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Titolo:
INTERNAL BETA-TURN HYDRATION - CRYSTALLOGRAPHIC EVIDENCE AND MOLECULAR-DYNAMICS SIMULATION
Autore:
DINOLA A; GAVUZZO E; MAZZA F; POCHETTI G; ROCCATANO D;
Indirizzi:
CNR,IST STRUTTURIST CHIM,CPN 10 I-00016 MONTEROTONDO ITALY CNR,IST STRUTTURIST CHIM I-00016 MONTEROTONDO ITALY UNIV ROMA LA SAPIENZA,DIPARTIMENTO CHIM I-00185 ROME ITALY UNIV LAQUILA,DIPARTIMENTO CHIM I-67010 LAQUILA ITALY
Titolo Testata:
Journal of physical chemistry
fascicolo: 23, volume: 99, anno: 1995,
pagine: 9625 - 9631
SICI:
0022-3654(1995)99:23<9625:IBH-CE>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
LEU-PHE-OME; ALPHA-HELIX; REVERSE TURNS; PEPTIDE; WATER; CONFORMATION; RESIDUES; CHEMOATTRACTANTS; PROTEINS; SEGMENTS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
A. Dinola et al., "INTERNAL BETA-TURN HYDRATION - CRYSTALLOGRAPHIC EVIDENCE AND MOLECULAR-DYNAMICS SIMULATION", Journal of physical chemistry, 99(23), 1995, pp. 9625-9631

Abstract

The X-ray structure analysis of the monohydrate phase of the peptide For-Met-Leu-Delta(2)Phe-Phe-OMe has revealed that the type-II beta-turn supported by the 4 --> 1 H-bond, expected for the backbone containing the alpha,beta-unsaturated residue Delta(2)Phe, has been modified bythe water molecule. The water prevents the 4 --> 1 H-bond between MetCO and Phe NH groups, forming a H-bonded bridge between these groups and causing significant modification of the secondary structure. The hydrated beta-turn found in the crystal can be an interesting static model useful for the comprehension of the internal hydration mechanism of beta-turns, secondary structures largely present in globular proteins, but generally distributed only on their surface. The internal hydration, with a H-bonded water bridge and modification of the secondary structure, differs from the most common external hydration, where the externally bound water does not cause modification of secondary structure. In order to verify whether the internally hydrated beta-turn couldbe found even in solution, a molecular dynamics simulation has been performed. The results show that the two forms, the beta-turn with the 4 --> 1 H-bond and that with the H-bonded water bridge, do not differ substantially in their energy values. Moreover, no high-energy barrierprevents interconversion between the two forms. The internal beta-turn hydration presents strong analogies with the internally hydrated helical peptide segments found in oligopeptides and proteins.

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Documento generato il 20/10/20 alle ore 05:16:06