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1.
P. R. health sci. j ; 18(4): 363-7, dez. 1999. ilus, tab, graf
Article in English | LILACS | ID: lil-260829

ABSTRACT

This brief report describes the isolation and initial characterization of revertants to the most severe temperature sensitive folding mutant known. The revertants or suppressors may describe amino acid interactions that occur during the folding of the P22 tailspike polypeptide chain. Results indicate that several different types of suppressors may have been obtained.


Subject(s)
/genetics , Genes, Suppressor/genetics , Glycoside Hydrolases/genetics , Mutation , Protein Folding , Viral Tail Proteins/genetics
2.
P. R. health sci. j ; 18(2): 105-15, jun. 1999. ilus, tab
Article in English | LILACS | ID: lil-255644

ABSTRACT

This review describes the use of a simple genetic system that has provided important insight into the process of folding and, of its flipside, that of protein aggregation. These studies make use of the tail protein of the bacterial virus P22 which infects Salmonella typhimurium. This folding system serves as a model for a number protein structural elements and may also provide important insights into disease-related protein folding defects at a time when an increasing number of diseases are being shown to be due to protein folding alterations


Subject(s)
Humans , /genetics , In Vitro Techniques , Protein Folding , Viral Tail Proteins/genetics , Amino Acids/genetics , Amino Acids/metabolism , /physiology , DNA, Viral/genetics , Hydrolysis , Mutation , Protein Conformation , Salmonella typhimurium/virology
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