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Literature DB >> 2238041

Halophilic proteins and the influence of solvent on protein stabilization.

Abstract

Competition between protein-solvent and protein-protein interactions is arguably the most important contributing factor to polypeptide folding in general. A study of halophilic proteins, correlating their stability and solution structures in different conditions, focuses on the effects of a high salt solvent. A mechanism is proposed to explain how these proteins have adapted to such an extreme environment.

Entities: Chemical Disease

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Year: 1990 PMID： 2238041 DOI： 10.1016/0968-0004(90)90068-m

Source DB: PubMed Journal: Trends Biochem Sci ISSN： 0968-0004 Impact factor: 13.807

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Cited

14 in total

1. Production of α-amylase fromHalobacterium halobium.

Authors: S Patel; N Jain; D Madamwar
Journal: World J Microbiol Biotechnol Date: 1993-01 Impact factor: 3.312

2. Further thermal characterization of an aspartate aminotransferase from a halophilic organism.

Authors: F J Muriana; M C Alvarez-Ossorio; A M Relimpio
Journal: Biochem J Date: 1994-03-01 Impact factor: 3.857

3. Reverse micelles in organic solvents: a medium for the biotechnological use of extreme halophilic enzymes at low salt concentration.

Authors: Frutos C Marhuenda-Egea; Sonsoles Piera-Velázquez; Chiquinquirá Cadenas; Eduardo Cadenas
Journal: Archaea Date: 2002-09 Impact factor: 3.273

4. N5,N10-methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri.

Authors: A R Klein; J Breitung; D Linder; K O Stetter; R K Thauer
Journal: Arch Microbiol Date: 1993 Impact factor: 2.552

5. Molecular processes in biological thermosensation.

Authors: I Digel; P Kayser; G M Artmann
Journal: J Biophys Date: 2008-05-12

6. Partial sequence of the gene for a serine protease from a halophilic archaeum Haloferax mediterranei R4, and nucleotide sequences of 16S rRNA encoding genes from several halophilic archaea.

Authors: M Kamekura; Y Seno
Journal: Experientia Date: 1993-07-05

Halophilic proteins and the influence of solvent on protein stabilization.

1. Production of α-amylase fromHalobacterium halobium.

2. Further thermal characterization of an aspartate aminotransferase from a halophilic organism.

3. Reverse micelles in organic solvents: a medium for the biotechnological use of extreme halophilic enzymes at low salt concentration.

4. N5,N10-methenyltetrahydromethanopterin cyclohydrolase from the extremely thermophilic sulfate reducing Archaeoglobus fulgidus: comparison of its properties with those of the cyclohydrolase from the extremely thermophilic Methanopyrus kandleri.

5. Molecular processes in biological thermosensation.

6. Partial sequence of the gene for a serine protease from a halophilic archaeum Haloferax mediterranei R4, and nucleotide sequences of 16S rRNA encoding genes from several halophilic archaea.

7. Genes for tryptophan biosynthesis in the halophilic archaebacterium Haloferax volcanii: the trpDFEG cluster.

8. Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii.

9. Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface.

Review 10. A decade and a half of protein intrinsic disorder: biology still waits for physics.