Billeter M, Kline A D, Braun W, Huber R, Wüthrich K
Institut für Molekularbiologie und Biophysik Eidenössische Technische Hochschule-Hönggerberg, Zürich, Switzerland.
J Mol Biol. 1989 Apr 20;206(4):677-87. doi: 10.1016/0022-2836(89)90575-5.
The three-dimensional structure of the alpha-amylase inhibitor Tendamistat determined by nuclear magnetic resonance in aqueous solution is compared with the Tendamistat crystal structure refined at 2.0 A resolution. Between the two independently obtained structures the root-mean-square distances are 1.05 A for the backbone atoms N, C alpha and C', 1.25 A for the backbone and the interior side-chains, and 1.84 A for all heavy atoms. These numbers show that the interior of the molecule is nearly identical in the two states. Near the protein surface a small number of local differences between the two structures were identified. In most surface areas the solution structure appears more disordered than the crystal structure, with the exception of Tyr15, which was not observed in the X-ray diffraction.
通过核磁共振在水溶液中测定的α-淀粉酶抑制剂田抗淀粉酶素的三维结构，与在2.0埃分辨率下精修的田抗淀粉酶素晶体结构进行了比较。在这两个独立获得的结构之间，主链原子N、Cα和C′的均方根距离为1.05埃，主链和内部侧链的均方根距离为1.25埃，所有重原子的均方根距离为1.84埃。这些数据表明，分子内部在两种状态下几乎是相同的。在蛋白质表面附近，鉴定出了两种结构之间的少量局部差异。在大多数表面区域，溶液结构看起来比晶体结构更无序，但Tyr15除外，它在X射线衍射中未被观察到。
