Tompa Peter, Han Kyou-Hoon, Bokor Mónika, Kamasa Pawel, Tantos Ágnes, Fritz Beáta, Kim Do-Hyoung, Lee Chewook, Verebélyi Tamás, Tompa Kálmán
Institute of Enzymology, Research Center for Natural Sciences, Hungarian Academy of Sciences, Budapest 1117, Hungary.
Genome Editing Research Center, Division of Biomedical Science, Korea Research Institute of Bioscience and Biotechnology (KRIBB), Daejeon 34141; Department of Nano & Bioinformatics, University of Science and Technology (UST), Daejeon 34113, Korea.
BMB Rep. 2016 Sep;49(9):497-501. doi: 10.5483/bmbrep.2016.49.9.037.
Wide-line 1H NMR intensity and differential scanning calorimetry measurements were carried out on the intrinsically disordered 73-residue full transactivation domain (TAD) of the p53 tumor suppressor protein and two peptides: one a wild type p53 TAD peptide with a helix pre-structuring property, and a mutant peptide with a disabled helix-forming propensity. Measurements were carried out in order to characterize their water and ion binding characteristics. By quantifying the number of hydrate water molecules, we provide a microscopic description for the interactions of water with a wild-type p53 TAD and two p53 TAD peptides. The results provide direct evidence that intrinsically disordered proteins (IDPs) and a less structured peptide not only have a higher hydration capacity than globular proteins, but are also able to bind a larger amount of charged solute ions. [BMB Reports 2016; 49(9): 497-501].
对p53肿瘤抑制蛋白的73个残基的内在无序全反式激活结构域（TAD）以及两条肽段进行了宽线¹H NMR强度和差示扫描量热法测量：一条是具有螺旋预构象特性的野生型p53 TAD肽段，另一条是螺旋形成倾向丧失的突变肽段。进行这些测量是为了表征它们与水和离子的结合特性。通过量化水合水分子的数量，我们对水与野生型p53 TAD以及两条p53 TAD肽段之间的相互作用进行了微观描述。结果提供了直接证据，表明内在无序蛋白（IDP）和结构较少的肽段不仅比球状蛋白具有更高的水合能力，而且还能够结合大量带电荷的溶质离子。[《BMB报告》2016年；49(9): 497 - 501]
