Abstract
Specific and interchangeable association of α-helix chains by hydrophobic and ionic interaction is discussed mainly for the assembly of αn, βn and γn subchains into various laminin isoforms. Sequence of laminin subchains suggests that the hydrophobic surface of α-helix formed by non-polar amino acids at positions a and d in (abcdefg)n heptad repeat is major force of interchain interaction but the ionic edges formed by charged amino acids at positions e and g determine the specificity of interaction.
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