Abstract
In recent years, the protein-folding problem has attracted the attention of molecular biologists. Efforts have focused on developing heuristic and energy-based algorithms to predict the three-dimensional structure of a protein from its amino acid sequence. We have applied a series of heuristic algorithms to the sequence of human growth hormone. A family of five structures which are generically right-handed fourfold alpha-helical bundles are found from an investigation of approximately 10(8) structures. A plausible receptor binding site is suggested. Independent crystallographic analysis confirms some aspects of these predictions. These methods only deal with the "core" structure, and conformations of many residues are not defined. Further work is required to identify a unique set of coordinates and to clarify the topological alternative available to alpha-helical proteins.
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