DSpace
 

DSpace at IIT Bombay >
IITB Publications >
Article >

Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/10359

Title: Understanding the relationship between the primary structure of proteins and their amyloidogenic propensity: clues from inclusion body formation
Authors: IDICULA-THOMAS, S
BALAJI, PV
Keywords: fibril formation
secondary structure
aggregation rates
alpha-helices
scrapie prion
in-vitro
sequence
peptide
beta
disease
Issue Date: 2005
Publisher: OXFORD UNIV PRESS
Citation: PROTEIN ENGINEERING DESIGN & SELECTION, 18(4), 175-180
Abstract: 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.
URI: http://dx.doi.org/10.1093/protein/gzi022
http://dspace.library.iitb.ac.in/xmlui/handle/10054/10359
http://hdl.handle.net/10054/10359
ISSN: 1741-0126
Appears in Collections:Article

Files in This Item:

There are no files associated with this item.

View Statistics

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback