Abstract
The proposal by Pauling and his coworkers (1951) of an atomic model for the structure of the alpha helix stimulated research in several areas of protein chemistry. It excited chemists as few discoveries have before or since, giving impetus to structural modeling efforts that resulted in the structure of DNA 2 years later, and in a whole new field of structural biology within two decades. Pauling’s feat pointed out the importance of understanding the conformation of the peptide group itself, rather than building models based on idealized helical structures. Working on the same problem, Bragg et al. (1950) failed to produce a structure of comparable elegance because they were unaware the peptide bond was planar (Crick, 1988). The alpha helix could be identified in the diffraction patterns from crystals of the globular proteins myoglobin and hemoglobin, as well as in the classical “α” patterns from fibrous proteins like keratin and synthetic polypeptides, poly(γ-l-glutamate) being the first to show the α pattern (Elliott, 1967).
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Kallenbach, N.R., Lyu, P., Zhou, H. (1996). CD Spectroscopy and the Helix-Coil Transition in Peptides and Polypeptides. In: Fasman, G.D. (eds) Circular Dichroism and the Conformational Analysis of Biomolecules. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2508-7_7
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