Abstract
Physical chemistry includes the study of how atoms come together to form molecules, and how combinations of molecules can interact with one another to form aggregates, crystals, and macromolecules. One of the most challenging problems in the area of macromolecules is the problem of protein structure, the problem of finding the “code” that specifies how a given amino acid sequence gives rise to a three-dimensional protein structure, such as an enzyme, with a highly specific biochemical function. This problem has been already attacked with considerable success using NMR methods, through studies of the folding-unfolding of polypeptides and proteins.1 Another important facet of the problem of protein structure, and the evolution of protein structures, concerns the manner in which amino acid sequences corresponding to exons, are assembled as structural units (“modules”) to form three-dimensional structures with specific functions.2
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© 1986 Plenum Press, New York
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McConnell, H.M., Frey, T., Anglister, J., Whittaker, M. (1986). Diversity of Molecular Recognition: The Combining Sites of Monoclonal Anti Spin Label Antibodies. In: Bradbury, E.M., Nicolini, C. (eds) NMR in the Life Sciences. NATO ASI Series, vol 107. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8178-5_7
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DOI: https://doi.org/10.1007/978-1-4684-8178-5_7
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