Ivanov Iu D, Bukharina N S, Frantsuzov P A, Krokhin N V, Kanashenko S L, Archakov A I
Biomed Khim. 2013 Jul-Aug;59(4):378-87. doi: 10.18097/pbmc20135904378.
Atomic force microscopy with two types of probes - standard (radius of curvature R approximately 10 nm) and supersharp (R approximately 2 nm)- was used to determine CYP102A1oligomeric state. CYP102A1 images were obtained in a liquid, air and vacuum environment using the standard probes, also a ratio of monomers to oligomers (alpha) of CYP102A1 were determined as alpha=0.48:0.52. At the same time use of standard probes did not allow to resolve the structure of these oligomers. Supersharp probes allowed to obtain the data about the monomers to oligomers ratio, and also about the dimers/trimers/tetramers ratio in air and vacuum. So, a ratio alpha of CYP102A1 in liquid can be determined by the standard probes, and an oligomeric state of protein can be specified by the supersharp probes.
使用两种类型的探针——标准探针（曲率半径R约为10纳米）和超尖探针（R约为2纳米）的原子力显微镜来确定CYP102A1的寡聚状态。使用标准探针在液体、空气和真空环境中获取CYP102A1图像，同时确定CYP102A1单体与寡聚体的比例（α）为α = 0.48:0.52。同时，使用标准探针无法解析这些寡聚体的结构。超尖探针能够获取关于空气和真空中单体与寡聚体比例以及二聚体/三聚体/四聚体比例的数据。因此，液体中CYP102A1的比例α可通过标准探针确定，而蛋白质的寡聚状态可由超尖探针明确。
