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Protein Folding: Part II—Energy Landscapes and Protein Dynamics

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Book cover Fundamentals of Neurodegeneration and Protein Misfolding Disorders

Part of the book series: Biological and Medical Physics, Biomedical Engineering ((BIOMEDICAL))

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Abstract

In thinking about how a protein might look in its three-dimensional fully folded form, Hsien Wu had envisioned it as forming a crystalline solid composed of repeated folded structural elements. That hope for simplicity by him and everyone else was effectively dashed by the pioneering studies of Kendrew and Perutz. Studies carried out later by Frederic Richards (1925–2009) [who solved the third ever protein structure in 1967, that of ribonuclease S] and others on packing densities confirmed part of Wu’s depiction. There were few if any large voids in the protein interior, and the overall protein densities were indeed consistent with that of an organic compound in the crystalline state, but one without repeating regularities. However, when examined at a finer scale it turns out that the interiors are quite variable in their packing and do not resemble a tightly fit-together jigsaw puzzle so much as a randomly packed sets of nuts and bolts. The packing is; in fact, loose enough to permit a variety of movements.

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    Martin Beckerman

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Beckerman, M. (2015). Protein Folding: Part II—Energy Landscapes and Protein Dynamics. In: Fundamentals of Neurodegeneration and Protein Misfolding Disorders. Biological and Medical Physics, Biomedical Engineering. Springer, Cham. https://doi.org/10.1007/978-3-319-22117-5_3

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