pi-Turns: types,systematics and the context of their occurrence in protein structures |
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Authors: | Bhaskar Dasgupta Pinak Chakrabarti |
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Affiliation: | (1) Bioinformatics Centre, Bose Institute, Calcutta, India;(2) Department of Biochemistry, Bose Institute, Calcutta, India |
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Abstract: | Background For a proper understanding of protein structure and folding it is important to know if a polypeptide segment adopts a conformation inherent in the sequence or it depends on the context of its flanking secondary structures. Turns of various lengths have been studied and characterized starting from three-residue γ-turn to six-residue π-turn. The Schellman motif occurring at the C-terminal end of α-helices is a classical example of hydrogen bonded π-turn involving residues at (i) and (i+5) positions. Hydrogen bonded and non-hydrogen bonded β- and α-turns have been identified previously; likewise, a systematic characterization of π-turns would provide valuable insight into turn structures. |
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