Circular dichroism studies on synthetic peptides corresponding to the cleavage site region of precursor proteins

Laxma Reddy, G. ; Nagaraj, R. (1987) Circular dichroism studies on synthetic peptides corresponding to the cleavage site region of precursor proteins International Journal of Peptide and Protein Research, 29 (4). pp. 497-503. ISSN 0367-8377

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Official URL: http://onlinelibrary.wiley.com/doi/10.1111/j.1399-...

Related URL: http://dx.doi.org/10.1111/j.1399-3011.1987.tb02276.x

Abstract

The conformations of synthetic peptides which span the region in which the precursor part of proteins (signal sequences) destined for export are cleaved by signal peptidases, were investigated by circular dichroism spectroscopy. Pentapeptides comprising amino acids only from the carboxy-terminus of signal sequences or the amino terminus of the mature protein do not have any preferred conformation in a variety of solvents. Octa- and nonapeptides containing amino acids from the carboxy-terminal protion of signal sequences and the amino-terminus of the mature portions of precursor proteins tend to adopt β-turn conformations in trifluoroethanol and micelles of sodium dodecylsulphate. Hence, in addition to the distribution of amino acids with small side chains at the carboxy terminus of signal sequences, it is conceivable that signal peptidases also recognize a β-turn conformation in the cleavage site region of precursor proteins.

Item Type:Article
Source:Copyright of this article belongs to Munksgaard International Publishers.
Keywords:Cleavage Site Region; Precursor Proteins; Signal Peptidase; Synthetic Peptides; Beta-turn
ID Code:23910
Deposited On:01 Dec 2010 12:56
Last Modified:09 Jun 2011 08:44

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