Somogyi B, Matkó J, Rosenberg A
Department of Biophysics, University Medical School of Debrecen, Hungary.
Acta Biochim Biophys Hung. 1988;23(2):135-48.
By using our model, described in the preceding paper, we investigate the effect of tri-N-acetylglucosamine binding on lysozyme. Furthermore, we reprocess the recently published data (Biochemistry, 1985, 24, 1342) on the effect of different inhibitors on adenosine deaminase. For lysozyme, the inhibitor binding decreases the dynamic accessibility of Trp-108 by changing the dynamics of the protein region separating the buried Trp-108 from the solvent. The reprocessed data on adenosine deaminase-inhibitor systems indicate that the inhibitors which presumably stabilize different (ground or transient) states alter the protein dynamics in both a qualitatively and quantitatively different manner in good agreement with the thermodynamic data of inhibitor binding. Our approach allows us to conclude that ligand induced changes of protein dynamics are not uniform and usually depend on where the protein-ligand complex is situated along the reaction coordinate (or phase-space) and are not localized to the protein groups building up the binding center.
通过使用我们在前一篇论文中描述的模型，我们研究了三 - N - 乙酰葡糖胺结合对溶菌酶的影响。此外，我们重新处理了最近发表的关于不同抑制剂对腺苷脱氨酶影响的数据（《生物化学》，1985年，第24卷，第1342页）。对于溶菌酶，抑制剂结合通过改变将埋藏的色氨酸 - 108与溶剂分隔开的蛋白质区域的动力学，降低了色氨酸 - 108的动态可及性。关于腺苷脱氨酶 - 抑制剂系统的重新处理数据表明，推测稳定不同（基态或瞬态）状态的抑制剂以定性和定量上不同的方式改变蛋白质动力学，这与抑制剂结合的热力学数据高度一致。我们的方法使我们能够得出结论，配体诱导的蛋白质动力学变化并不均匀，通常取决于蛋白质 - 配体复合物在反应坐标（或相空间）上的位置，并且并不局限于构成结合中心的蛋白质基团。
