Abstract
X-RAY crystallographic studies on globular proteins reveal segments whose secondary structure resembles the α-helical and β-extended chain models for polypeptides1,2. These segments are joined by relatively nonregular structures, particularly at bends in the polypeptide backbone. Marked departures from some of the structural criteria laid down in the development of the α and β models occur in these non-regular segments. Here, neither the principle of the constancy of the angles of rotation ψ and φ around the Cα–C′ and N–Cα bonds respectively3 of the peptide bond (I), nor that of maximisation of hydrogen bond formation between peptide groups applies4.
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JONES, R. Regular and non-regular secondary structure in globular proteins. Nature 272, 185–187 (1978). https://doi.org/10.1038/272185a0
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DOI: https://doi.org/10.1038/272185a0
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