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- W2024368431 endingPage "542" @default.
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- W2024368431 abstract "The reverse turn, involving four consecutive amino acids, as a tertiary conformation in globular proteins is defined in terms of dihedral angles, the C(1) (alpha)...C(4) (alpha) distance and the O(1)...H-N(4) hydrogen bond distance. In seven proteins we find 125 examples of turns, comprising 33% of the amino acids in these proteins, as compared with 34% of the residues forming helices and only 17% forming beta-sheets. The amino-acid compositions of turns, helices, and beta-sheets are analyzed in some detail. We find Asn and Gly mainly in turns, Pro in turns (and at the beginning of helices), and Glu in helices. In these turns a statistical survey indicates that 19% of Asp residues are in the first position, 33% of Pro residues are in the second position, 24% of Asn residues are in the third position, and 26% of Trp residues are in the fourth position." @default.
- W2024368431 created "2016-06-24" @default.
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- W2024368431 date "1973-02-01" @default.
- W2024368431 modified "2023-10-10" @default.
- W2024368431 title "The Reverse Turn as a Polypeptide Conformation in Globular Proteins" @default.
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- W2024368431 doi "https://doi.org/10.1073/pnas.70.2.538" @default.
- W2024368431 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/433301" @default.
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