Articles written in Journal of Chemical Sciences
Volume 97 Issue 1 July 1986 pp 71-75 Organic
A synthetic peptide corresponding to the signal sequence of
Volume 98 Issue 5-6 June 1987 pp 479-485
Proteins destined for regions other than the cytoplasm in cells have to cross at least one membrane barrier before reaching their proper destination. Almost all such proteins are initially biosynthesized as precursors with signal sequences at the amino terminus. Signal sequences are essential and also sufficient for proteins to be targeted to membranes and also for translocation across membranes. One striking feature that is clearly evident amongst signal sequences of secretory proteins is a positively charged amino terminus followed by a region comprising 10–12 very hydrophobic amino acids. The structural and physico-chemical properties of signal sequences have been analysed. On the basis of the analyses it is proposed that the structural feature of a positively charged amino terminal region followed by a hydrophobic stretch of amino acids, rather than a conformational one, is recognised by components of the cells export machinery. It is also postulated that signal sequences insert in the lipid bilayer of the translocation competent membrane after targeting. The presence of the signal sequence results in the formation of local ‘defects’ in the bilayer which have a role in translocation of proteins across membranes.
Volume 109 Issue 5 October 1997 pp 319-323 Organic
The synthesis of peptides by manual solid-phase methods requiring very small volume of solvents at different steps is described. The syntheses have been carried out on polystyrene-based resins using fluorenylmethoxy carboxyl chemistry. All reactions were carried out in vials, of capacity 1.2 or 6 ml, with gentle stirring. The volumes of solvents used were 1–2 ml for each operation. The crude peptides after cleavage from the resin were reasonably pure. The total volume of solvents required for the entire synthesis is substantially less as compared to volumes required in semi-automated and fully automated peptide synthesizers which renders the described method cost-effective.
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