Abstract
There are plenty of possible structures (isomers) for a given number of atoms; their number quickly becoming astronomical for larger molecules. Usually only some of these structures (low-energy ones) play a role in experiments. However, in the theoretical description of the system in principle, all these structures have to be taken into account, a very costly adventure. Therefore, one of the challenges of chemistry (as well as of physics, biology, etc.) is the multiple minima problem, that is, how to identify the low-energy structures without calculating all possible configurations of atoms. The protein folding is given as an example of overcoming the multiple minima problem.
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Acknowledgments
The author is very indebted to Professor Andrzej Koliński, Department of Chemistry, University of Warsaw, for kindly providing his results prior to publication.
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Piela, L. (2009). Challenging the Multiple Minima Problem: Example of Protein Folding. In: Leszczynski, J., Shukla, M. (eds) Practical Aspects of Computational Chemistry. Springer, Dordrecht. https://doi.org/10.1007/978-90-481-2687-3_5
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DOI: https://doi.org/10.1007/978-90-481-2687-3_5
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