S. Dhar, D. K. Rana, A. Pal and S. C. Bhattacharya, “Photobehavior and Docking Simulations of Drug within Macromolecules: Binding of an Antioxidative Isoquino- lindione to a Serine Protease and Albumin Proteins,” Journal of Photochemistry and Photobiology B: Biology, Vol. 129, 2013, pp. 69-77.
http://dx.doi.org/10.1016/j.jphotobiol.2013.09.007
[2]
D. Ray, B. K. Paul and N. Guchhait, “Differential Binding Modes of Anti-Cancer, Anti-HIV Drugs Belonging to Isatin Family with a Model Transport Protein: A Joint Refinement from Spectroscopic and Molecular Modeling Approaches,” Journal of Photochemistry and Photobiology B: Biology, Vol. 127, 2013, pp. 18-27.
http://dx.doi.org/10.1016/j.jphotobiol.2013.09.007
[3]
W.J. Hua, J. D. Biggs, Y. Zhang, D. Healion, H. Ren and S. Mukamel, “Multiple Core and Vibronic Coupling Effects in Attosecond Stimulated X-Ray Raman Spectroscopy,” Journal of Chemical Theory and Computation, Vol. 9, No. 12, 2013, pp. 5479-5489.
http://dx.doi.org/10.1021/ct400767g
[4]
A. J. Gesquiere, “Optical Properties and Spectroscopy of Nanomaterials,” Journal of the American Chemical Society, Vol. 132, No. 10, 2010, pp. 3637-3638.
http://dx.doi.org/10.1021/ja101350v
[5]
I. Sizov, M. Rahman, B. Gelmont, M. L. Norton and T. Globus, “Sub-THz Spectroscopic Characterization of Vibrational Modes in Artificially Designed DNA Monocrystal,” Chemical Physics, Vol. 425, 2013, pp. 121-125.
http://dx.doi.org/10.1016/j.chemphys.2013.08.015
[6]
S. Roy, P. A. Covert, W. R. FitzGerald and D. K. Hore, “Biomolecular Structure at Solid-Liquid Interfaces as Revealed by Nonlinear Optical Spectroscopy,” Chemical Reviews, 2014. http://dx.doi.org/10.1021/cr400418b
[7]
M. Vithanage, A. U. Rajapaksha, X. M. Dou, N. S. Bolan, J. E. Yang and Y. S. Ok, “Surface Complexation Modeling and Spectroscopic Evidence of Antimony Adsorption on Iron-Oxide-Rich Red Earth Soils,” Journal of Colloid and Interface Science, Vol. 406, 2013, pp. 217-224.
http://dx.doi.org/10.1016/j.jcis.2013.05.053
[8]
M. Brucale, B. Schuler and B. Samorì, “Single-Molecule Studies of Intrinsically Disordered Proteins,” Chemical Reviews, 2014. http://dx.doi.org/10.1021/cr400297g
[9]
J. Xu, J. Z. H. Zhang and Y. Xiang, “Molecular Dynamics Simulation and Computational Two-Dimensional Infrared Spectroscopic Study of Model Amyloid β-Peptide Oligomers,” The Journal of Physical Chemistry A, Vol. 117, No. 29, 2013, pp. 6373-6379.
http://dx.doi.org/10.1021/jp403748z
[10]
L. M. da Costa, S. R. Stoyanov, S. Gusarov, P. R. Seidl, J. W. M. Carneiro and A. Kovalenko, “Computational Study of the Effect of Dispersion Interactions on the Thermochemistry of Aggregation of Fused Polycyclic Aromatic Hydrocarbons as Model Asphaltene Compounds in Solution,” The Journal of Physical Chemistry A, Vol. 118, No. 5, 2014, pp. 896-908.
http://dx.doi.org/10.1021/jp408005h
[11]
K. T. Cheung, Y. Foo, C. H. To and J. A. Zapien, “Towards FDTD Modeling of Spectroscopic Ellipsometry Data at Large Angles of Incidence,” Applied Surface Science, Vol. 281, 2013, pp. 2-7.
http://dx.doi.org/10.1016/j.apsusc.2012.12.144
[12]
S. Jana, S. Dalapati, S. Ghosh and N. Guchhait, “Binding Interaction between Plasma Protein Bovine Serum Albumin and Flexible Charge Transfer Fluorophore: A Spectroscopic Study in Combination with Molecular Docking and Molecular Dynamics Simulation,” Journal of Photochemistry and Photobiology A: Chemistry, Vol. 231, No. 1, 2012, pp. 19-27.
http://dx.doi.org/10.1016/j.jphotochem.2011.12.002
[13]
M. Memarpoor-Yazdi and H. Mahaki, “Probing the Interaction of Human Serum Albumin with Vitamin B2 (Riboflavin) and l-Arginine (l-Arg) Using Multi-Spectroscopic, Molecular Modeling and Zeta Potential Techniques,” Journal of Luminescence, Vol. 136, 2013, pp. 150-159. http://dx.doi.org/10.1016/j.jlumin.2012.11.016