Characteristic features of amino acid residues in coiled-coil protein structures

• Published in: Biophysical chemistry Vol. 111; no. 2; pp. 95 - 103
• Main Authors: Gromiha, M.Michael, Parry, David A.D.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.10.2004
• Subjects: Amino Acids - chemistry; Amino Acids - metabolism; B′-factor; Cation–π interactions; Coiled coils; Conformational parameters; Hydrophobic and Hydrophilic Interactions; Hydrophobicity; Inter-residue contacts; Protein Folding; Protein Structure, Secondary; Proteins - chemistry; Proteins - metabolism; Thermodynamics; Conformational parameters; Inter-residue contacts; B′-factor; Hydrophobicity; Coiled coils; Cation–π interactions
• ISSN: 0301-4622; 1873-4200
• DOI: 10.1016/j.bpc.2004.05.001

Detailed analyses of protein structures provide an opportunity to understand conformation and function in terms of amino acid sequence and composition. In this work, we have systematically analyzed the characteristic features of the amino acid residues found in α-helical coiled-coils and, in so doing, have developed indices for their properties, conformational parameters, surrounding hydrophobicity and flexibility. As expected, there is preference for hydrophobic (Ala, Leu), positive (Lys, Arg) and negatively (Glu) charged residues in coiled-coil domains. However, the surrounding hydrophobicity of residues in coiled-coil domains is significantly less than that for residues in other regions of coiled-coil proteins. The analysis of temperature factors in coiled-coil proteins shows that the residues in these domains are more stable than those in other regions. Further, we have delineated the medium- and long-range contacts in coiled-coil domains and compared the results with those obtained for other (non-coiled-coil) parts of the same proteins and non-coiled-coil helical segments of globular proteins. The residues in coiled-coil domains are largely influenced by medium-range contacts, whereas long-range interactions play a dominant role in other regions of these same proteins as well as in non-coiled-coil helices. We have also revealed the preference of amino acid residues to form cation–π interactions and we found that Arg is more likely to form such interactions than Lys. The parameters developed in this work can be used to understand the folding and stability of coiled-coil proteins in general.