Hardaway L A, Brems D N, Beals J M, MacKenzie N E
Department of Pharmaceutical Sciences, University of Arizona, Tucson 85721.
Biochim Biophys Acta. 1994 Sep 21;1208(1):101-3. doi: 10.1016/0167-4838(94)90165-1.
Comparative analysis of the 1H-NMR spectra of human insulin shows that in the presence of the allosteric ligand, phenol, the tertiary structure of the protein is altered as evidenced by the decreased rate of amide hydrogen-deuterium exchange. In particular, exchange of amide protons in residues of the B-chain helix (B9-B20) are significantly affected suggesting either a stabilization of this helix or a reduction in the solvent accessibility of the helix in the R-state. This paper exemplifies the exchange rates of two amides (ValB18 and TyrB16) from this helix which decrease by approximately 400-fold as a result of this ligand induced conformational transition.
人胰岛素的1H-NMR谱的比较分析表明，在变构配体苯酚存在的情况下，蛋白质的三级结构发生了改变，这一点可由酰胺氢-氘交换速率降低得到证明。特别是，B链螺旋（B9-B20）残基中的酰胺质子交换受到显著影响，这表明该螺旋要么得到稳定，要么在R态下螺旋的溶剂可及性降低。本文举例说明了该螺旋中两个酰胺（ValB18和TyrB16）的交换速率，由于这种配体诱导的构象转变，其交换速率降低了约400倍。
