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Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: clues from inclusion body formation

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Title Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: clues from inclusion body formation
 
Creator IDICULA-THOMAS, S
BALAJI, PV
 
Subject fibril formation
secondary structure
aggregation rates
alpha-helices
scrapie prion
in-vitro
sequence
peptide
beta
disease
aliphatic index
discordant stretch
instability index
sheet propensity
thermostability
 
Description Amyloid formation is dependent to a considerable extent on the amino acid sequence of the protein. The present study delineates certain sequence-dependent features that are correlated with amyloidogenic propensity. The analyses indicate that amyloid formation is favored by lower thermostability and increased half-life of the protein. There seems to be a certain degree of bias in the composition of order-promoting amino acids in the case of amyloidogenic proteins. Based on these parameters, a prediction function for the amyloidogenic propensity of proteins has been created. The prediction function has been found to rationalize the reported effect of certain mutations on amyloid formation. It seems that a higher sheet propensity of residues that constitute the first seven residues of a helical structure in a protein might increase the propensity for a helix to sheet transition in that region under denaturing conditions.
 
Publisher OXFORD UNIV PRESS
 
Date 2011-08-22T07:33:53Z
2011-12-26T12:56:15Z
2011-12-27T05:44:41Z
2011-08-22T07:33:53Z
2011-12-26T12:56:15Z
2011-12-27T05:44:41Z
2005
 
Type Article
 
Identifier PROTEIN ENGINEERING DESIGN & SELECTION, 18(4), 175-180
1741-0126
http://dx.doi.org/10.1093/protein/gzi022
http://dspace.library.iitb.ac.in/xmlui/handle/10054/10359
http://hdl.handle.net/10054/10359
 
Language en