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Structural Patterns in α Helices and β Sheets in Globular Proteins

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Secondary structural elements like α-helix and β-sheet constitute the major components of proteins. Here we present a systematic position wise analysis of the structural and sequence characteristics of alpha-helices and beta-sheets. Helix and sheet are found to follow a complementary distribution pattern along the protein chain length. We have calculated the conformational parameters of the amino acids forming helices and sheets. Other properties like hydrophobicity, temperature-factor and relative entropy are found to be correlated with the distribution pattern of these secondary structures. This gives an insight about the conservation or variation of the secondary structure in proteins, which may have significant implications on de novo protein design.

Keywords: Complementary distribution pattern; conformational parameter; hydrophobicity; relative entropy; temperature factor

Document Type: Research Article


Publication date: 2009-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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