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The role of phenylalanine 31 in maintaining the conformational stability of ribonuclease P2 from Sulfolobus solfataricus under extreme conditions of temperature and pressure.

Abstract：

:Ribonuclease P2 from the thermophilic archaebacterium Sulfolobus solfataricus is a small protein (7 kDa) with a known three-dimensional structure. Inspection of the structure and molecular dynamics simulation reveal that three aromatic residues (Phe5, Phe31, and Tyr33) from the hydrophobic core have a strong van der Waals interaction energy. We studied the thermodynamics of the heat, cold, and pressure-induced protein conformational changes of the wild type and of the F31A and F31Y mutants by analyzing the protein UV absorbance in the fourth derivative mode. The wild-type protein was extremely stable under all conditions of temperature and pressure. Heat and cold denaturation of both mutants, as well as denaturation by pressure of the F31A mutant, led to significant blue shifts of the derivative spectrum, indicating increased solvent exposure of Tyr33. For the F31Y mutant, high pressure (400 MPa) protected the protein against thermal denaturation. This study, probing the properties of the hydrophobic aromatic core, complements a thermal unfolding study which probes the overall structural changes [Knapp, S., Karshikoff, A., Berndt, K. D., Christova, P., Atanasov, B., & Ladenstein, R. (1996) J. Mol. Biol. 264,1132-1144]. The differences observed in response to extremes of temperature, pressure, and pH may be rationalized by an unfolding mechanism involving larger parts of the peripheral protein while the integrity of the hydrophobic core is maintained.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Mombelli E,Afshar M,Fusi P,Mariani M,Tortora P,Connelly JP,Lange R

doi

10.1021/bi970467v

subject

Has Abstract

pub_date

1997-07-22 00:00:00

pages

8733-42

issue

29

eissn

0006-2960

issn

1520-4995

pii

bi970467v

journal_volume

36

pub_type

杂志文章

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