Abstract
The folding of polypeptide chains into compact globular structures is often the supposition for the expression of their biological function in the cell. The determination of the spatial arrangement of the peptide chain by X-ray diffraction has given the most important information on the static properties of globular proteins. But the elucidation of the pathways of folding, the magnitude of the different thermodynamic forces involed, and the kinetics of such processes are still in a relatively early stage of investigation.
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Pohl, F.M. (1977). Protein Folding and Unfolding. In: Pecht, I., Rigler, R. (eds) Chemical Relaxation in Molecular Biology. Molecular Biology Biochemistry and Biophysics, vol 24. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81117-3_8
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DOI: https://doi.org/10.1007/978-3-642-81117-3_8
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