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Titolo:
Protein stability in extremophilic Archaea
Autore:
Scandurra, R; Consalvi, V; Chiaraluce, R; Politi, L; Engel, PC;
Indirizzi:
Univ Rome La Sapienza, Dipartimento Sci Biochim A RossiFanelli, I-00185 Rome, Italy Univ Rome La Sapienza Rome Italy I-00185 ssiFanelli, I-00185 Rome, Italy Univ Coll Dublin, Conway Inst Biomol & Biomed Res, Dept Biochem, Dublin 4,Ireland Univ Coll Dublin Dublin Ireland 4 ed Res, Dept Biochem, Dublin 4,Ireland
Titolo Testata:
FRONTIERS IN BIOSCIENCE
, volume: 5, anno: 2000,
pagine: D787 - D795
SICI:
1093-9946(20000901)5:<D787:PSIEA>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
FURIOSUS GLUTAMATE-DEHYDROGENASE; HALOPHILIC MALATE-DEHYDROGENASE; ACTIVE CITRATE SYNTHASE; CRYSTAL-STRUCTURE; PYROCOCCUS-FURIOSUS; HYPERTHERMOPHILIC ARCHAEON; THERMAL-STABILITY; ION-PAIRS; 3-ISOPROPYLMALATE DEHYDROGENASE; 2.5-ANGSTROM RESOLUTION;
Keywords:
protein stability; extremophiles; electrostatic interactions; halophiles; psychrophiles; thermophiles; review;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
64
Recensione:
Indirizzi per estratti:
Indirizzo: Scandurra, R Univ Rome La Sapienza, Dipartimento Sci Biochim A RossiFanelli, Piazzale Aldo Moro 5, I-00185 Rome, Italy Univ Rome La Sapienza PiazzaleAldo Moro 5 Rome Italy I-00185
Citazione:
R. Scandurra et al., "Protein stability in extremophilic Archaea", FRONT BIOSC, 5, 2000, pp. D787-D795

Abstract

Extremophilic microorganisms have adapted their molecular machinery to grow and thrive under the most adverse enviromental conditions. These microorganisms have found their natural habitat at the boiling and freezing point of water, in high salt concentration and at extreme pH values. The extremophilic proteins, selected by Nature to withstand this evolutionary pressure, represent a wide research field for scientists from different disciplines and the study of the determinants of their stability has been an important task for basic and applied research. A surprising conclusion emerges from these studies: there are no general rules to achieve protein stabilization. Each extremophilic protein adopts various strategies and the outstanding adaptation to extreme temperature and solvent conditions is realized through the same weak electrostatic and hydrophobic interactions among the ordinary amino acid residues which are also responsible for the proper balance between protein stability and flexibility in mesophilic proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 20:53:45