Interactions that regulate the helical fold in proteins

Cid, H.; Gazitua F.; Bunster, M

Keywords: sequence, stability, acid, enzyme, protein, structure, acids, peptide, interaction, hormones, disulfide, article, secondary, folding, leucine, pancreatic, dipole, amino, alanine, Structure,, synthetic, carboxy, terminal, Muramidase

Abstract

Several factors that may contribute to the stabilization of the helical structure in proteins, detected in studies made on short synthetic peptides, have been reported. Some of them are presence of alanine or leucine, ionic-pair bonding, stabilization of the helical dipole moment by appropriate charges at the helix N- and C-caps, and aromatic interactions of amino acids located at positions i, i + 4. An analysis of 54 helical structures from 12 proteins showed that all these stabilizing factors were also present in proteins, but the influence of any of them had a different weight, according to the distribution of the hydrophobic and hydrophilic amino acid residues in the helical sequence. The role of non-sequence depending interactions in helical stability, such as presence of disulfide bridges, or bonding of helical residues to substrate and/or cofactors, was also analysed.

Más información

Título de la Revista: Biological Research
Volumen: 29
Número: 2
Editorial: Springer
Fecha de publicación: 1996
Página de inicio: 213
Página final: 225
URL: http://www.scopus.com/inward/record.url?eid=2-s2.0-0030011037&partnerID=q2rCbXpz