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Molecular bases of protein halotolerance
- Source :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1844:850-858
- Publication Year :
- 2014
- Publisher :
- Elsevier BV, 2014.
-
Abstract
- Halophilic proteins are stable and function at high salt concentration. Understanding how these molecules maintain their fold stable and avoid aggregation under harsh conditions is of great interest for biotechnological applications. This mini-review describes what is known about the molecular determinants of protein halotolerance. Comparisons between the sequences of halophilic/non-halophilic homologous protein pairs indicated that Asp and Glu are significantly more frequent, while Lys, Ile and Leu are less frequent in halophilic proteins. Homologous halophilic and non-halophilic proteins have similar overall structure, secondary structure content, and number of residues involved in the formation of H-bonds. On the other hand, on the halophilic protein surface, a decrease of nonpolar residues and an increase of charged residues are observed. Particularly, halophilic adaptation correlates with an increase of Asp and Glu, compensated by a decrease of basic residues, mainly Lys, on protein surface. A thermodynamic model, that provides a reliable explanation of the salt effect on the conformational stability of globular proteins, is presented.
- Subjects :
- Models, Molecular
Salinity
Globular protein
Amino Acids, Acidic
Static Electricity
Biophysics
Biology
Biochemistry
Protein Structure, Secondary
Analytical Chemistry
Evolution, Molecular
Structure-Activity Relationship
Protein structure
Molecular evolution
Molecular Biology
Protein secondary structure
halophilic proteins
chemistry.chemical_classification
Protein Stability
Amino Acids, Basic
Proteins
Hydrogen Bonding
Protein superfamily
Adaptation, Physiological
Halophilic archaea
Halophile
Thermodynamic model
chemistry
Halotolerance
Thermodynamics
Amino Acids, Branched-Chain
Subjects
Details
- ISSN :
- 15709639
- Volume :
- 1844
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- Accession number :
- edsair.doi.dedup.....4e50b81beaf4a7ae1f5eb31ec8d679af