Desaturases: Extreme cold adaptation and the biological significance in Antarctic organisms
Entry ID: UNISA_DIFARMA_DESATURASES

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Summary
Abstract: It has been shown that thermal stability of proteins is modified by very minor changes in the amino acid (aa) sequence. For ex., for malic dehydrogenase and other proteins, a single aa substitution results in alteration in thermal stability. Among other proteins, those involved in temperature adaptation, heat shock and desaturase proteins are particularly important for the comprehension, at a ... View entire text
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Geographic Coverage
Spatial coordinates   
  N: -74.5   S: -77.5   E: 166.3   W: 165.0

Temporal Coverage
Start Date: 1986-12-10
Stop Date: 2006-12-04
ISO Topic Category
Data Set Progress
IN WORK
Data Center
Universita Degli Studi Di Salerno, Dipartimento di Scienze Farmaceutiche, Italy Supplemental Info
Data Center URL: http://www.difarma.unisa.it/

Data Center Personnel
Name: BRUNO MARESCA
Phone: +39-089/96 97 58
Fax: +39-089/96 96 02
Email: bmaresca at unisa.it
Contact Address:
Via Ponte don Melillo
City: FISCIANO (SALERNO)
Postal Code: 84084
Country: Italy
Personnel
Role: INVESTIGATOR
Phone: +39-089/96 97 58
Fax: +39-089/96 96 02
Email: bmaresca at unisa.it
Contact Address:
Via Ponte don Melillo
City: FISCIANO (SALERNO)
Postal Code: 84084
Country: Italy
Publications/References
Porta, A, T. and B. Maresca. A unique cys-cys bond in the first -elix domain of a delta-9-desaturase gene of the Antartic fish Chionodraco hamatus and Thrematomus bernacchii confers cold adaptation to the protein. In preparation 2006 Submitted to J. Experimental Biology
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Creation and Review Dates
DIF Creation Date: 2008-03-06
Last DIF Revision Date: 2008-03-14
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