Packing and recognition of protein structural elements: a new approach applied to the 4-helix bundle of myohemerythrin.
We present a novel search strategy for determining the optimal packing of protein secondary structure elements. The approach is based on conformational energy optimization using a predetermined set of side chain rotamers and appropriate methods for sampling the conformational space of peptide fragments having fixed backbone geometries. An application to the 4-helix bundle of myohemerythrin is presented. It is shown that the conformations of the amino acid side chains are largely determined at the level of helix pairs and that superposition of these results can be used to construct the full bundle. The final solution obtained, taking into account restrictions due to the lateral amphiphilicity of the helices, differs from the native structure by only a 20 degrees rotation of a single helix.
Tufféry
P
P
Laboratoire de Biochimie Théorique, Institut de Biologie Physico-Chimique, Paris, France.
Lavery
R
R
D000595:Amino Acid Sequence; D006422:Hemerythrin / Q000031:analogs & derivatives* / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D006422:Hemerythrin; C008571:myohemerythrin