A key factor in the properties of biological molecules is their structure. This research has focused on the problem of protein structure prediction due to the critical role of peptides and proteins in the normal biological functionality of cells and organisms. At sufficiently low temperatures, though not always, the structure of the minimal free energy corresponds to the global minimum of its force field (FF) -- its Potential Energy Surface (PES), which is a function expressing the potential energy interactions inside the molecule. The problem of predicting the native (or folded ) structure of a polypeptide given its sequence or some unfolded structure is the problem of finding that global minimum. This problem is computationally hard because we know that a polypeptide's PES has an estimated number of minima, exponential on its sequence length.
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Dissertation corner
Goldstein, Moshe
Follow ACM SIGEVOlution
, Volume 4 (3)
Association for Computing Machinery – Feb 1, 2010
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