Protein Folding and Misfolding: A Perspective from Theory

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Protein Folding and Misfolding: A Perspective from Theory

Protein folding is a problem of great importance in both life sciences and biotechnology industries. A very large number of distinct conformations exist for the polypeptide chain of which a protein molecule is composed. The protein spends most of its time in the native conformation, which spans only an infinitesimal fraction of the entire configuration space. The general perception has been that the protein folding problem is a grand challenge that will require many supercomputer years to solve. During the past few years, there has been a great increase in the level of interest in protein folding. This is due in part to the challenge of the human genome project and in part to the development of experimental methods that provide more details about the folding process. One conclusion from the measurements is that an essential part of the folding process, the search for an ordered globule with many attributes of the native structures, is composed within the dead time. Much less is known about the features of the potential surface governing the non-native portion of configurational space involved in protein folding. This includes a wide range of structures that may differ by tens of angstroms and be separated by significant energy barriers


Citation: Naeem A, Khan TA, Fazili NA (2015) Protein Folding and Misfolding: A Perspective from Theory. J Glycomics Lipidomics 5:128 doi: 10.4172/2153-0637.1000128

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