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Conformational properties of the N-terminal residues of S-peptide. I. The ribonuclease S′ system

✍ Scribed by Bruno Filippi; Gianfranco Borin; Ugo Anselmi; Fernando Marchiori

Publisher
Wiley (John Wiley & Sons)
Year
1978
Tongue
English
Weight
1019 KB
Volume
17
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The contribution of the 1–6 N‐terminal sequence to the conformational properties of the S‐peptide (the 1–20 sequence of ribonuclease A) was assessed by determining in the ribonuclease S′ system the helical content and the binding capability of synthetic [Orn^10^]‐S‐peptide analogs, in which lysine^1^, glutamic^2^ and threonine^3^ were progressively deleted, alanine^4^ and alanine^5^were alternatively replaced by serine, and alanine^6^ was substituted by serine or proline. Both the deletion of the three N‐terminal residues and the alanine^6^/proline replacement produces the loss of the helical structure up to lysine^7^. No or minor effects are found in all other cases. From the comparison of the binding data, the energy for the conformational stabilization of the N‐terminal region was calculated to amount to 1.4 kcal/mol. The results are discussed in comparison with the known x‐ray data of the enzyme, with some predictive rules of secondary structure which were applied to this region and with the known phylogenetic variance of the residues in this region.

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