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- W2077895595 abstract "The first three residues at the N terminus of the α-helix are called N1, N2 and N3. We surveyed 2102 α-helix N termini in 298 high-resolution, non-homologous protein crystal structures for N1, N2 and N3 amino acid and side-chain rotamer propensities and hydrogen-bonding patterns. We find strong structural preferences that are unique to these sites. The rotamer distributions as a function of amino acid identity and position in the helix are often explained in terms of hydrogen-bonding interactions to the free N1, N2 and N3 backbone NH groups. Notably, the “good N2” amino acid residues Gln, Glu, Asp, Asn, Ser, Thr and His preferentially form i,i or i,i + 1 hydrogen bonds to the backbone, though this is hindered by good N-caps (Asp, Asn, Ser, Thr and Cys) that compete for these hydrogen bond donors. We find a number of specific side-chain to side-chain interactions between N1 and N2 or between the N-cap and N2 or N3, such as Arg(N-cap) to Asp(N2). The strong energetic and structural preferences found for N1, N2 and N3, which differ greatly from positions within helix interiors, suggest that these sites should be treated explicitly in any consideration of helical structure in peptides or proteins." @default.
- W2077895595 created "2016-06-24" @default.
- W2077895595 creator A5000626384 @default.
- W2077895595 creator A5005165880 @default.
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- W2077895595 date "1999-03-01" @default.
- W2077895595 modified "2023-10-12" @default.
- W2077895595 title "Side-chain structures in the first turn of the α-helix 1 1Edited by J. M. Thornton" @default.
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- W2077895595 doi "https://doi.org/10.1006/jmbi.1998.2549" @default.
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