Steiner T
Institut für Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195 Berlin, Germany.
Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):584-8. doi: 10.1107/s090744499701500x.
In crystalline Tyr-Tyr-Leu monohydrate, an aromatic-(i+1) amine hydrogen bond is observed, that is a weak hydrogen-bond-type interaction between an aromatic side chain and N-H of the next peptide group in the main chain. Unlike the better investigated aromatic-(i+2) amine hydrogen bonds, which can adopt almost ideal geometries, the geometry of the discussed interaction is very distorted because of steric constraints. Presumably, this kind of weak hydrogen bond is only formed as a last resort if N-H finds it impossible to engage in the much stronger conventional hydrogen bonding with O-atom acceptors.
在结晶水合酪氨酸-酪氨酸-亮氨酸中，观察到一种芳香族-(i+1)胺氢键，即芳香族侧链与主链中下一个肽基团的N-H之间的一种弱氢键型相互作用。与研究得更充分的芳香族-(i+2)胺氢键不同，后者可以采用几乎理想的几何构型，由于空间位阻，所讨论的这种相互作用的几何构型非常扭曲。据推测，只有当N-H无法与氧原子受体形成更强的传统氢键时，这种弱氢键才会作为最后的手段形成。
