References
- Asgharzadeh, S., Shareghi, B., Farhadian, S., & Tirgir, F. (2019). Effect of free L-cysteine on the structure and function of α-chymotrypsin. Journal of Molecular Liquids, 280, 79–86. https://doi.org/https://doi.org/10.1016/j.molliq.2019.01.144
- Borowitzka, L. (1985). Glycerol and other carbohydrate osmotic effectors. In Transport processes, iono- and osmoregulation (pp. 437–453). Springer.
- Büttner, M., & Sauer, N. (2000). Monosaccharide transporters in plants: Structure, function and physiology. Biochimica et Biophysica Acta (BBA) – Biomembranes, 1465(1–2), 263–274. https://doi.org/https://doi.org/10.1016/S0005-2736(00)00143-7
- Chintapalli, S. V., Bhardwaj, G., Patel, R., Shah, N., Patterson, R. L., van Rossum, D. B., Anishkin, A., & Adams, S. H. (2015). Molecular dynamic simulations reveal the structural determinants of fatty acid binding to oxy-myoglobin. PloS One, 10(6), e0128496. https://doi.org/https://doi.org/10.1371/journal.pone.0128496
- Delavari, B., Saboury, A. A., Atri, M. S., Ghasemi, A., Bigdeli, B., Khammari, A., Maghami, P., Moosavi-Movahedi, A. A., Haertlé, T., & Goliaei, B. (2015). Alpha-lactalbumin: A new carrier for vitamin D3 food enrichment. Food Hydrocolloids, 45, 124–131. https://doi.org/https://doi.org/10.1016/j.foodhyd.2014.10.017
- Divsalar, A., Saboury, A. A., Ahadi, L., Zemanatiyar, E., & Mansouri-Torshizi, H. (2010). Investigation of effects of newly synthesized Pt(II) complex against human serum albumin and leukemia cell line of K562. BMB Reports, 43(11), 766–771. https://doi.org/https://doi.org/10.5483/BMBRep.2010.43.11.766
- Eslami-Farsani, R., Shareghi, B., Farhadian, S., & Momeni, L. (2020). Insight into the binding of glycerol with myoglobin: Spectroscopic and MD simulation approach. International Journal of Biological Macromolecules, 159, 433–443. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2020.04.065
- Essa, H., Magner, E., Cooney, J., & Hodnett, B. (2007). Influence of pH and ionic strength on the adsorption, leaching and activity of myoglobin immobilized onto ordered mesoporous silicates. Journal of Molecular Catalysis B: Enzymatic, 49(1–4), 61–68. https://doi.org/https://doi.org/10.1016/j.molcatb.2007.07.005
- Farhadian, S., Shareghi, B., & Saboury, A. A. (2017). Exploring the thermal stability and activity of α-chymotrypsin in the presence of spermine. Journal of Biomolecular Structure & Dynamics, 35(2), 435–448. https://doi.org/https://doi.org/10.1080/07391102.2016.1147984
- Farhadian, S., Shareghi, B., Saboury, A. A., & Momeni, L. (2016). Counteraction of lactose on the thermal stability and activity of α-chymotrypsin: Thermodynamic, kinetic and docking studies. RSC Advances, 6(76), 72201–72212. https://doi.org/https://doi.org/10.1039/C6RA11833J
- Ghalandari, B., Divsalar, A., Saboury, A. A., Haertlé, T., Parivar, K., Bazl, R., Eslami-Moghadam, M., & Amanlou, M. (2014). Spectroscopic and theoretical investigation of oxali–palladium interactions with β-lactoglobulin. Spectrochimica Acta. Part A, Molecular and Biomolecular Spectroscopy, 118, 1038–1046. https://doi.org/https://doi.org/10.1016/j.saa.2013.09.126
- Hansson, T., Oostenbrink, C., & van Gunsteren, W. (2002). Molecular dynamics simulations. Current Opinion in Structural Biology, 12(2), 190–196. https://doi.org/https://doi.org/10.1016/S0959-440X(02)00308-1
- Hu, X., Yu, Z., & Liu, R. (2013). Spectroscopic investigations on the interactions between isopropanol and trypsin at molecular level. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 108, 50–54. https://doi.org/https://doi.org/10.1016/j.saa.2013.01.072
- Jamal, S., Poddar, N. K., Singh, L. R., Dar, T. A., Rishi, V., & Ahmad, F. (2009). Relationship between functional activity and protein stability in the presence of all classes of stabilizing osmolytes. The FEBS Journal, 276(20), 6024–6032. https://doi.org/https://doi.org/10.1111/j.1742-4658.2009.07317.x
- Jing, M., Song, W., & Liu, R. (2016). Binding of copper to lysozyme: Spectroscopic, isothermal titration calorimetry and molecular docking studies. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 164, 103–109. https://doi.org/https://doi.org/10.1016/j.saa.2016.04.008
- Koutsopoulos, S., Patzsch, K., Bosker, W. T., & Norde, W. (2007). Adsorption of trypsin on hydrophilic and hydrophobic surfaces. Langmuir: The ACS Journal of Surfaces and Colloids, 23(4), 2000–2006. https://doi.org/https://doi.org/10.1021/la062238s
- Lakowicz, J. R. (2013). Principles of fluorescence spectroscopy. Springer Science & Business Media.
- Leandro, P., Lechner, M. C., de Almeida, I. T., & Konecki, D. (2001). Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system. Molecular Genetics and Metabolism, 73(2), 173–178. https://doi.org/https://doi.org/10.1006/mgme.2001.3172
- Liu, F.-F., Ji, L., Zhang, L., Dong, X.-Y., & Sun, Y. (2010). Molecular basis for polyol-induced protein stability revealed by molecular dynamics simulations. The Journal of Chemical Physics, 132(22), 225103. https://doi.org/https://doi.org/10.1063/1.3453713
- Liu, W., Liu, J.-P., Zou, L.-Q., Zhang, Z.-Q., Liu, C.-M., Liang, R.-H., Xie, M.-Y., & Wan, J. (2014). Stability and conformational change of methoxypolyethylene glycol modification for native and unfolded trypsin. Food Chemistry, 146, 278–283. https://doi.org/https://doi.org/10.1016/j.foodchem.2013.09.067
- Lu, S.-Y., Jiang, Y.-J., Lv, J., Wu, T.-X., Yu, Q.-S., & Zhu, W.-L. (2010). Molecular docking and molecular dynamics simulation studies of GPR40 receptor–agonist interactions. Journal of Molecular Graphics & Modelling, 28(8), 766–774. https://doi.org/https://doi.org/10.1016/j.jmgm.2010.02.001
- Mishra, R., Seckler, R., & Bhat, R. (2005). Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes how well are protein folding and stability aspects coupled? The Journal of Biological Chemistry, 280(16), 15553–15560. https://doi.org/https://doi.org/10.1074/jbc.M410947200
- Moghaddam, M. M., Pirouzi, M., Saberi, M. R., & Chamani, J. (2014). Comparison of the binding behavior of FCCP with HSA and HTF as determined by spectroscopic and molecular modeling techniques. Luminescence: The Journal of Biological and Chemical Luminescence, 29(4), 314–331. https://doi.org/https://doi.org/10.1002/bio.2546
- Moradi, M., Divsalar, A., Saboury, A., Ghalandari, B., & Harifi, A. (2015). Inhibitory effects of deferasirox on the structure and function of bovine liver catalase: A spectroscopic and theoretical study. Journal of Biomolecular Structure & Dynamics, 33(10), 2255–2266. https://doi.org/https://doi.org/10.1080/07391102.2014.999353
- Moradi, S., Shareghi, B., Saboury, A. A., & Farhadian, S. (2020). Investigation on the interaction of acid phosphatase with putrescine using docking, simulations methods and multispectroscopic techniques. International Journal of Biological Macromolecules, 150, 90–101. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2020.02.057
- Morris, G. M., Huey, R., Lindstrom, W., Sanner, M. F., Belew, R. K., Goodsell, D. S., & Olson, A. J. (2009). AutoDock4 and AutoDockTools4: Automated docking with selective receptor flexibility. Journal of Computational Chemistry, 30(16), 2785–2791. https://doi.org/https://doi.org/10.1002/jcc.21256
- Ong, H. N., Arumugam, B., & Tayyab, S. (2009). Succinylation-induced conformational destabilization of lysozyme as studied by guanidine hydrochloride denaturation. Journal of Biochemistry, 146(6), 895–904. https://doi.org/https://doi.org/10.1093/jb/mvp136
- Ordway, G. A., & Garry, D. J. (2004). Myoglobin: An essential hemoprotein in striated muscle. The Journal of Experimental Biology, 207(Pt 20), 3441–3446. https://doi.org/https://doi.org/10.1242/jeb.01172
- Palaniappan, V., & Bocian, D. F. (1994). Acid-induced transformations of myoglobin. Characterization of a new equilibrium heme-pocket intermediate. Biochemistry, 33(47), 14264–14274. https://doi.org/https://doi.org/10.1021/bi00251a039
- Patra, D., & Barakat, C. (2012). Time-resolved fluorescence study during denaturation and renaturation of curcumin–myoglobin complex. International Journal of Biological Macromolecules, 50(4), 885–890. https://doi.org/https://doi.org/10.1016/j.ijbiomac.2012.02.010
- Paul, B. K., Bhattacharjee, K., Bose, S., & Guchhait, N. (2012). A spectroscopic investigation on the interaction of a magnetic ferrofluid with a model plasma protein: Effect on the conformation and activity of the protein. Physical Chemistry Chemical Physics, 14(44), 15482–15493. https://doi.org/https://doi.org/10.1039/c2cp42415k
- Prasad, S., & Roy, I. (2010). Effect of disaccharides on the stabilization of bovine trypsin against detergent and autolysis. Biotechnology Progress, 26(3), 627–635. https://doi.org/https://doi.org/10.1002/btpr.367
- Saeidifar, M., Mansouri-Torshizi, H., & Saboury, A. A. (2015). Biophysical study on the interaction between two palladium(II) complexes and human serum albumin by multispectroscopic methods. Journal of Luminescence, 167, 391–398. https://doi.org/https://doi.org/10.1016/j.jlumin.2015.07.016
- Shareghi, B., Farhadian, S., Zamani, N., Salavati-Niasari, M., Moshtaghi, H., & Gholamrezaei, S. (2015). Investigation the activity and stability of lysozyme on presence of magnetic nanoparticles. Journal of Industrial and Engineering Chemistry, 21, 862–867. https://doi.org/https://doi.org/10.1016/j.jiec.2014.04.024
- Stepankova, V., Bidmanova, S., Koudelakova, T., Prokop, Z., Chaloupkova, R., & Damborsky, J. (2013). Strategies for stabilization of enzymes in organic solvents. ACS Catalysis, 3(12), 2823–2836. https://doi.org/https://doi.org/10.1021/cs400684x
- Stryer, L., Tymoczko, J., & Berg, J. (2011). Biochemistry: A short course. WH Freeman & Company.
- Sudha, N., Chandrasekaran, S., Sameena, Y., & Israel, V. (2015). Mode of encapsulation of linezolid by β-cyclodextrin and its role in bovine serum albumin binding. Carbohydrate Polymers, 115, 589–597.
- Timasheff, S. N. (2002). Protein–solvent preferential interactions, protein hydration, and the modulation of biochemical reactions by solvent components. Proceedings of the National Academy of Sciences of the United States of America, 99(15), 9721–9726. https://doi.org/https://doi.org/10.1073/pnas.122225399
- Venkatesu, P., Lee, M.-J., & Lin, H-m. (2007). Thermodynamic characterization of the osmolyte effect on protein stability and the effect of GdnHCl on the protein denatured state. The Journal of Physical Chemistry B, 111(30), 9045–9056. https://doi.org/https://doi.org/10.1021/jp0701901
- Vignesh, G., Manojkumar, Y., Sugumar, K., & Arunachalam, S. (2015). Spectroscopic investigation on the interaction of some polymer–cobalt(III) complexes with serum albumins. Journal of Luminescence, 157, 297–302. https://doi.org/https://doi.org/10.1016/j.jlumin.2014.08.045
- Wittenberg, J. B., & Wittenberg, B. A. (2003). Myoglobin function reassessed. The Journal of Experimental Biology, 206(Pt 12), 2011–2020. https://doi.org/https://doi.org/10.1242/jeb.00243
- Wu, J., Zhao, C., Lin, W., Hu, R., Wang, Q., Chen, H., Li, L., Chen, S., & Zheng, J. (2014). Binding characteristics between polyethylene glycol (PEG) and proteins in aqueous solution. Journal of Materials Chemistry B, 2(20), 2983–2992. https://doi.org/https://doi.org/10.1039/c4tb00253a
- Zhao, F.-Q., & Keating, A. F. (2007). Functional properties and genomics of glucose transporters. Current Genomics, 8(2), 113–128. https://doi.org/https://doi.org/10.2174/138920207780368187
- Zong, W., Liu, R., Sun, F., Teng, Y., Fang, X., & Chai, J. (2011). A new strategy to identify and eliminate the inner filter effects by outer filter technique. Journal of Fluorescence, 21(3), 1249–1254. https://doi.org/https://doi.org/10.1007/s10895-010-0806-y