The Nest is a type of protein structural motif. It is a small recurring anion-binding feature of both proteins and peptides.[1][2][3][4][5][6][7][8][9] Each consists of the main chain atoms of three consecutive amino acid residues. The main chain NH groups bind the anions while the side chain atoms are often not involved. Proline residues lack NH groups so are rare in nests. About one in 12 of amino acid residues in proteins, on average, belongs to a nest.
^Watson, JD; Milner-White (2002). "A novel main-chain anion-binding site in proteins: The nest. A particular combination of phi,psi values in successive residues gives rise to anion-binding sites that occur commonly and are found often at functionally important regions". Journal of Molecular Biology. 315 (2): 171–182. doi:10.1006/jmbi.2001.5227. PMID11779237.
^Pal, D; Suhnel (2002). "New principles of protein structure: nests, eggs and what next?". Angew Chem Int Ed. 41 (24): 4663–4665. doi:10.1002/anie.200290009. PMID12481319.
^Pajewski, R; Ferdani (2005). "Cation Dependence of Chloride Ion Complexation by Open-Chained Receptor Molecules in Chloroform Solution". Journal of the American Chemical Society. 127 (51): 18281–18295. doi:10.1021/ja0558894. PMID16366583.
^Berkessel, A; Koch (2006). "Asymmetric enone epoxidation by solid-phase bound peptides: further evidence for catalyst helicity and catalytic activity of individual strands". Biopolymers. 84 (1): 90–96. doi:10.1002/bip.20413. PMID16283656.