Choi Jun-Ho, Raleigh Daniel, Cho Minhaeng
Department of Chemistry, Korea University, Seoul 136-701, Korea.
J Phys Chem Lett. 2011 Sep 1;2(17):2158-2162. doi: 10.1021/jz200980g.
The use of IR probes to monitor protein structure, deduce local electric field, and investigate the mechanism of enzyme catalysis and protein folding has attracted increasing attention. Here, the azidohomoalanine (Aha) is considered as a useful IR probe. The intricate details of the distinct effects of backbone peptide bonds and H-bonded water molecules on the azido stretch mode of the IR probe Aha were revealed by carrying out QM/MM MD simulations of two variants of the protein NTL9, NTL9-Met1Aha and NTL9-Ile4Aha and comparing the resulting simulated IR spectra with experiments.
使用红外（IR）探针监测蛋白质结构、推断局部电场以及研究酶催化和蛋白质折叠机制已引起越来越多的关注。在此，叠氮高丙氨酸（Aha）被认为是一种有用的红外探针。通过对蛋白质NTL9的两个变体NTL9-Met1Aha和NTL9-Ile4Aha进行量子力学/分子力学（QM/MM）分子动力学（MD）模拟，并将所得模拟红外光谱与实验结果进行比较，揭示了主链肽键和氢键结合的水分子对红外探针Aha的叠氮伸缩模式的不同影响的复杂细节。
