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Protein Engineering, Vol. 14, No. 5, 321-328, May 2001
© 2001 Oxford University Press

Side-chain conformations in 4-{alpha}-helical bundles

Vasiliki E. Fadouloglou1,2, Nicholas M. Glykos2 and Michael Kokkinidis1,2,3

1 Department of Biology, University of Crete, P.O. Box 2208, GR-71409 Heraklion and 2 Foundation for Research and Technology–Hellas, Institute of Molecular Biology and Biotechnology (IMBB), P.O. Box 1527, GR-71110 Heraklion, Crete, Greece

The distribution of the {chi}1, {chi}2 dihedral angles in a dataset consisting of 12 unrelated 4-{alpha}-helical bundle proteins was determined and qualitatively compared with that observed in globular proteins. The analysis suggests that the 4-{alpha}-helical bundle motif could occasionally impose steric constraints on side chains: (i) the side-chain conformations are limited to only a subset of the conformations observed in globular proteins and for some amino acids they are sterically more constrained than those in helical regions of globular proteins; (ii) aspartic acid and asparagine occasionally adopt rotamers that have not been previously reported for globular or helical proteins; (iii) some rotamers of tyrosine and isoleucine are predominantly or exclusively associated with hydrophobic core positions (a, d); (iv) mutations in the hydrophobic core occur preferentially between residue types which among other physicochemical properties also share a predominant rotamer.


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