Dartigalongue Thibault, Hache François
Laboratoire d'Optique et Biosciences-Centre National de la Recherche Scientifique-Institute National de la Sante et de la Recherche Medicale, Ecole Polytechnique, 91128 Palaiseau Cedex, France.
J Chem Phys. 2005 Nov 8;123(18):184901. doi: 10.1063/1.2041467.
A calculation of the circular dichroism (CD) spectra of carbon monoxy- and deoxy myoglobin is carried out in relation with a time-resolved CD experiment. The calculation is based on the polarizability theory and the parameters are adjusted to fit the experimental absorption and CD spectra. By performing the calculation for intermediate configurations of the protein, we are able to propose an explanation of the CD structure observed on a sub-100 ps time scale. The role of the proximal histidine is, in particular, clearly demonstrated in the first step of the myoglobin relaxation from its liganded to it deliganded form.
结合时间分辨圆二色性（CD）实验，对一氧化碳肌红蛋白和脱氧肌红蛋白的CD光谱进行了计算。该计算基于极化率理论，并对参数进行了调整以拟合实验吸收光谱和CD光谱。通过对蛋白质中间构型进行计算，我们能够对在亚100皮秒时间尺度上观察到的CD结构作出解释。特别是，在肌红蛋白从其配体形式转变为去配体形式的第一步弛豫过程中，近端组氨酸的作用得到了清晰的展现。
