Circular dichroism studies on the signal sequence of E. coli alkaline phosphatase indicate the presence of both α-helix and β-structure in hydrophobic environments

Laxma Reddy, G. ; Nagaraj, R. (1986) Circular dichroism studies on the signal sequence of E. coli alkaline phosphatase indicate the presence of both α-helix and β-structure in hydrophobic environments FEBS Letters, 202 (2). pp. 349-352. ISSN 0014-5793

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/001457...

Related URL: http://dx.doi.org/10.1016/0014-5793(86)80716-5

Abstract

The conformations of a synthetic peptide corresponding to the signal sequence of E. coli alkaline phosphatase, Lys-Gln-Ser-Thr-Ile-Ala-Leu-Ala-Leu-Leu-Pro-Leu-Leu-Phe-Thr-Pro-Val-Thr-Lys-Ala-OCH3, have been examined in different environments by circular dichroism spectroscopy. In trifluoroethanol, methanol and aqueous mixtures of these solvents, the signal peptide has largely random conformation (~80%) with small amounts of a-helix and β-structure. However, in micellar environment, there is a significant increase in ordered conformation with both α-helix and β-structure being present, unlike in other signal sequences reported in the literature, where only the α-helical conformation has been observed. Hence, an α-helical conformation may not be as stringent a requirement as overall hydrophobicity for recognition of signal sequences by the cell's export machinery.

Item Type:Article
Source:Copyright of this article belongs to Federation of European Biochemical Societies.
Keywords:CD; Signal Sequence; Helical Conformation; β-structure
ID Code:23518
Deposited On:25 Nov 2010 13:12
Last Modified:17 May 2016 07:20

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