A protein molecule is a covalent chain of amino acid residues. Although it is topologically linear, in physiological conditions it folds into a unique (though flexible) three-dimensional structure. This structure, which has been determined by x-ray crystallography and nuclear magnetic resonance for many proteins (Bernstein et al., 1977; Abola et al., 1987), is referred to as the native structure. As demonstrated by the experiments of Anfinsen and co-workers (Anfinsen et al., 1961; Anfinsen, 1973), at least some protein molecules, when denatured (unfolded) by disrupting conditions in their environment (such as acidity or high temperature) can spontaneously refold to their native structures when proper physiological conditions are restored. Thus, all of the information necessary to determine the native structure can be contained in the amino acid sequence.
CITATION STYLE
Ngo, J. T., Marks, J., & Karplus, M. (1994). Computational Complexity, Protein Structure Prediction, and the Levinthal Paradox. In The Protein Folding Problem and Tertiary Structure Prediction (pp. 433–506). Birkhäuser Boston. https://doi.org/10.1007/978-1-4684-6831-1_14
Mendeley helps you to discover research relevant for your work.