Investigating specificity of the anti-hypertensive inhibitor WNK463 against With-No-Lysine kinase family isoforms via multiscale simulations

References

• AlAmri, M. A., Kadri, H., Dhiani, B. A., Mahmood, S., Elzwawi, A., & Mehellou, Y. (2017). WNK signaling inhibitors as potential antihypertensive drugs. ChemMedChem, 12(20), 1677–1686. doi:10.1002/cmdc.201700425
   PubMed Web of Science ®Google Scholar
• Bayel Secinti, B., Tatar, G., & Taskin Tok, T. (2018). Determination of potential selective inhibitors for ROCKI and ROCKII isoforms with molecular modeling techniques: structure based docking, ADMET and molecular dynamics simulation. Journal of Biomolecular Structure and Dynamics, (in press) doi:10.1080/07.391102.2018.1491420
   PubMed Web of Science ®Google Scholar
• Beg, A., Khan, F. I., Lobb, K. A., Islam, A., Ahmad, F., & Hassan, M. I. (2018). High throughput screening, docking, and molecular dynamics studies to identify potential inhibitors of human calcium/calmodulin-dependent protein kinase IV. Journal of Biomolecular Structure and Dynamics, doi:10.1080/07391102.2018.1479310
   Web of Science ®Google Scholar
• Case, D. A., Betz, R. M., Cerutti, D. S., Cheatham, T. E., III, Darden, T. A., Duke, R. E., … Kollman, P. A. (2016). AMBER 2016. San Francisco, CA: University of California.
   Google Scholar
• Castañeda-Bueno, M., & Gamba, G. (2012). Mechanisms of sodium–chloride cotransporter modulation by angiotensin II. Current Opinion in Nephrology and Hypertension, 21(5), 516–522. doi:10.1097/MNH.0b013e32835571a4
   PubMed Web of Science ®Google Scholar
• Chaudhary, N., & Aparoy, P. (2017). Deciphering the mechanism behind the varied binding activities of COXIBs through Molecular Dynamic Simulations, MM-PBSA binding energy calculations and per-residue energy decomposition studies. Journal of Biomolecular Structure and Dynamics, 35, 868–882. doi:10.1080/07391102.2016.1165736
   PubMed Web of Science ®Google Scholar
• Chaudhry, A., Noor, A., Degagne, B., Baker, K., Bok, L., Brady, A., … Dyment, D. (2015). Phenotypic spectrum associated with PTCHD1 deletions and truncating mutations includes intellectual disability and autism spectrum disorder. Clinical Genetics, 88(3), 224–233. doi:10.1111/cge.12482
   PubMed Web of Science ®Google Scholar
• Chiga, M., Rai, T., Yang, S.-S., Ohta, A., Takizawa, T., Sasaki, S., & Uchida, S. (2008). Dietary salt regulates the phosphorylation of OSR1/SPAK kinases and the sodium chloride cotransporter through aldosterone. Kidney International, 74(11), 1403–1409. doi:10.1038/ki.2008.451
   PubMed Web of Science ®Google Scholar
• Darden, T., York, D., & Pedersen, L. (1993). Particle mesh Ewald: An N⋅ log (N) method for Ewald sums in large systems. The Journal of Chemical Physics, 98(12), 10089–10092. doi:10.1063/1.464397
   Web of Science ®Google Scholar
• de los Heros, P., Kahle, K. T., Rinehart, J., Bobadilla, N. A., Vázquez, N., San Cristobal, P., … Gamba, G. (2006). WNK3 bypasses the tonicity requirement for K-Cl cotransporter activation via a phosphatase-dependent pathway. Proceedings of the National Academy of Sciences USA, 103(6), 1976–1981. doi:10.1073/pnas.0510947103
   PubMed Web of Science ®Google Scholar
• Dhanasekaran, N. (1998). Cell signaling: an overview. Oncogene, 17(11 Reviews), 1329. doi:10.1038/sj.onc.1202170
   PubMed Web of Science ®Google Scholar
• Dhillon, A. S., Hagan, S., Rath, O., & Kolch, W. (2007). MAP kinase signalling pathways in cancer. Oncogene, 26(22), 3279. doi:10.1038/sj.onc.1210421
   PubMed Web of Science ®Google Scholar
• Dimke, H. (2011). Exploring the intricate regulatory network controlling the thiazide-sensitive NaCl cotransporter (NCC). Pflügers Archiv, 462(6), 767–777. doi:10.1007/s00424-011-1027-1
   PubMed Web of Science ®Google Scholar
• Duan, L., Feng, G., Wang, X., Wang, L., & Zhang, Q. (2017). Effect of electrostatic polarization and bridging water on CDK2–ligand binding affinities calculated using a highly efficient interaction entropy method. Physical Chemistry Chemical Physics, 19(15), 10140–10152. doi:10.1039/C7CP00841D
   PubMed Web of Science ®Google Scholar
• Eisenberg, D., Lüthy, R., & Bowie, J. U. (1997). [20] VERIFY3D: Assessment of protein models with three-dimensional profiles. Methods in Enzymology, 277, 396–404.
   PubMed Web of Science ®Google Scholar
• Genheden, S., & Ryde, U. (2015). The MM/PBSA and MM/GBSA methods to estimate ligand-binding affinities. Expert Opin Drug Discov, 10(5), 449–461. doi:10.1517/17460441.2015.1032936
   PubMed Web of Science ®Google Scholar
• Gohlke, H., Kiel, C., & Case, D. A. (2003). Insights into protein–protein binding by binding free energy calculation and free energy decomposition for the Ras–Raf and Ras–RalGDS complexes. Journal of Molecular Biology, 330(4), 891–913. doi:10.1016/S0022-2836(03)00610-7
   PubMed Web of Science ®Google Scholar
• Gouda, H., Kuntz, I. D., Case, D. A., & Kollman, P. A. (2003). Free energy calculations for theophylline binding to an RNA aptamer: comparison of MM‐PBSA and thermodynamic integration methods. Biopolymers: Original Research on Biomolecules, 68(1), 16–34. doi:10.1002/bip.10270
   PubMed Web of Science ®Google Scholar
• Hofinger, S., & Zerbetto, F. (2009). Introducing temperature dependence in an enhanced Poisson-Boltzmann approach. Chemical Physics Letters, 480, 313–317. doi:10.1016/j.cplett.2009.08.079
   Web of Science ®Google Scholar
• Huang, C.-L., Cha, S.-K., Wang, H.-R., Xie, J., & Cobb, M. H. (2007). WNKs: protein kinases with a unique kinase domain. Experimental & Molecular Medicine, 39(5), 565. doi:10.1038/emm.2007.62
   PubMed Web of Science ®Google Scholar
• Jakalian, A., Jack, D. B., & Bayly, C. I. (2002). Fast, efficient generation of high‐quality atomic charges. AM1‐BCC model: II. Parameterization and validation. Journal of Computational Chemistry, 23(16), 1623–1641. doi:10.1002/jcc.10128
   PubMed Web of Science ®Google Scholar
• Jayaram, B., Sprous, D., Young, M., & Beveridge, D. (1998). Free energy analysis of the conformational preferences of A and B forms of DNA in solution. Journal of the American Chemical Society, 120(41), 10629–10633. doi:10.1021/ja981307p
   Web of Science ®Google Scholar
• Jorgensen, W. L., Chandrasekhar, J., Madura, J. D., Impey, R. W., & Klein, M. L. (1983). Comparison of simple potential functions for simulating liquid water. The Journal of Chemical Physics, 79(2), 926–935. doi:10.1063/1.445869
   Web of Science ®Google Scholar
• Kahle, K. T., Rinehart, J., Ring, A., Gimenez, I., Gamba, G., Hebert, S. C., & Lifton, R. P. (2006). WNK protein kinases modulate cellular Cl − flux by altering the phosphorylation state of the Na-K-Cl and K-Cl cotransporters. Physiology, 21(5), 326–335. doi:10.1152/physiol.00015.2006
   PubMedGoogle Scholar
• Kar, P., & Knecht, V. (2012a). Energetic basis for drug resistance of HIV-1 protease mutants against amprenavir. Journal of Computer-Aided Molecular Design, 26(2), 215–232. doi:10.1007/s10822-012-9550-5
   PubMed Web of Science ®Google Scholar
• Kar, P., & Knecht, V. (2012d). Origin of decrease in potency of darunavir and two related antiviral inhibitors against HIV-2 compared to HIV-1 protease. The Journal of Physical Chemistry B, 116(8), 2605–2614. doi:10.1021/jp211768n
   PubMed Web of Science ®Google Scholar
• Kar, P., & Knecht, V. (2012b). Energetics of mutation-induced changes in potency of lersivirine against HIV-1 reverse transcriptase. The Journal of Physical Chemistry B, 116(22), 6269–6278. doi:10.1021/jp300818c
   PubMed Web of Science ®Google Scholar
• Kar, P., & Knecht, V. (2012c). Mutation-induced loop opening and energetics for binding of tamiflu to influenza N8 neuraminidase. The Journal of Physical Chemistry. B, 116(21), 6137–6149. doi:10.1021/jp3022612
   PubMed Web of Science ®Google Scholar
• Kar, P., Lipowsky, R., & Knecht, V. (2011). Importance of polar solvation for cross-reactivity of antibody and its variants with steroids. The Journal of Physical Chemistry. B, 115(23), 7661–7669. doi:10.1021/jp201538t
   PubMed Web of Science ®Google Scholar
• Kar, P., Seel, M., Weidemann, T., & Hofinger, S. (2009). Theoretical mimicry of biomembranes. FEBS Letters, 583(12), 1909–1915. doi:10.1016/j.febslet.2009.04.040
   PubMed Web of Science ®Google Scholar
• Karplus, M., & Kushick, J. N. (1981). Method for estimating the configurational entropy of macromolecules. Macromolecules, 14(2), 325–332. doi:10.1021/ma50003a019
   Web of Science ®Google Scholar
• Knighton, D. R., Zheng, J., Ten Eyck, L. F., Ashford, V. A., Xuong, N.-H., Taylor, S. S., & Sowadski, J. M. (1991). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science, 253(5018), 407–414. doi:10.1126/science.1862342
   PubMed Web of Science ®Google Scholar
• Kollman, P. A., Massova, I., Reyes, C., Kuhn, B., Huo, S., Chong, L., … Wang, W. (2000). Calculating structures and free energies of complex molecules: combining molecular mechanics and continuum models. Accounts of Chemical Research, 33(12), 889–897. doi:10.1021/ar000033j
   PubMed Web of Science ®Google Scholar
• Kräutler, V., Van Gunsteren, W. F., & Hünenberger, P. H. (2001). A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. Journal of Computational Chemistry, 22, 501–508. doi:10.1002/1096-987X(20010415)22:5<501::AID-JCC1021>3.0.CO;2-V
   Web of Science ®Google Scholar
• Kuenemann, M. A., & Fourches, D. (2018). Cheminformatics analysis of dynamic WNK‐inhibitor interactions. Molecular Informatics, 37(6–7), 1700138. doi:10.1002/minf.201700138
   Web of Science ®Google Scholar
• Kumar, A., Srivastava, G., Negi, A. S., & Sharma, A. (2019). Docking, molecular dynamics, binding energy-MM-PBSA studies of naphthofuran derivatives to identify potential dual inhibitors against BACE-1 and GSK-3β. Journal of Biomolecular Structure and Dynamics, 37(2), 275–290. doi:10.1080/07391102.2018.1426043
   PubMed Web of Science ®Google Scholar
• Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. Journal of Applied Crystallography, 26(2), 283–291. doi:10.1107/S0021889892009944
   Web of Science ®Google Scholar
• Li, J. J., Cheng, P., Tu, J., Zhai, H. L., & Zhang, X. Y. (2016). Enhancing specificity in the Janus kinases: a study on the thienopyridine JAK2 selective mechanism combined molecular dynamics simulation. Molecular Biosystems, 12(2), 575–587. doi:10.1039/C5MB00747J
   PubMedGoogle Scholar
• Lovell, S. C., Davis, I. W., Arendall, W. B., III, De Bakker, P. I., Word, J. M., Prisant, M. G., … Richardson, D. C. (2003). Structure validation by Cα geometry: ϕ, ψ and Cβ deviation. Proteins: Structure, Function, and Bioinformatics, 50(3), 437–450. doi:10.1002/prot.10286
   PubMed Web of Science ®Google Scholar
• Lybrand, T. P., McCammon, J. A., & Wipff, G. (1986). Theoretical calculation of relative binding affinity in host-guest systems. Proceedings of the National Academy of Sciences USA, 83(4), 833–835. doi:10.1073/pnas.83.4.833
   PubMed Web of Science ®Google Scholar
• Maier, J. A., Martinez, C., Kasavajhala, K., Wickstrom, L., Hauser, K. E., & Simmerling, C. (2015). ff14SB: improving the accuracy of protein side chain and backbone parameters from ff99SB. Journal of Chemical Theory and Computation, 11(8), 3696–3713. doi:10.1021/acs.jctc.5b00255
   PubMed Web of Science ®Google Scholar
• Majumdar, S., Basu, D., & Ghosh Dastidar, S. (2018). Conformational states of E7010 is complemented by microclusters of water inside the α, β-Tubulin core. Journal of Chemical Information and Modeling, (in press) doi:10.1021/acs.jcim.8b00538
   PubMed Web of Science ®Google Scholar
• Markosian, C., Di Costanzo, L., Sekharan, M., Shao, C., Burley, S. K., & Zardecki, C. (2018). Analysis of impact metrics for the Protein Data Bank. Scientific Data, 5, 180212. doi:10.1038/sdata.2018.212
   PubMed Web of Science ®Google Scholar
• Massova, I., & Kollman, P. A. (1999). Computational alanine scanning to probe protein − protein interactions: a novel approach to evaluate binding free energies. Journal of the American Chemical Society, 121(36), 8133–8143.
   Web of Science ®Google Scholar
• McCormick, J. A., & Ellison, D. H. (2011). The WNKs: atypical protein kinases with pleiotropic actions. Physiological Reviews, 91(1), 177–219. doi:10.1152/physrev.00017.2010
   PubMed Web of Science ®Google Scholar
• Moniz, S., Verissimo, F., Matos, P., Brazao, R., Silva, E., Kotevelets, L., … Jordan, P. (2007). Protein kinase WNK2 inhibits cell proliferation by negatively modulating the activation of MEK1/ERK1/2. Oncogene, 26(41), 6071. doi:10.1038/sj.onc.1210706
   PubMed Web of Science ®Google Scholar
• Moriguchi, T., Urushiyama, S., Hisamoto, N., Iemura, S-I., Uchida, S., Natsume, T., … Shibuya, H. (2005). WNK1 regulates phosphorylation of cation-chloride-coupled cotransporters via the STE20-related kinases, SPAK and OSR1. Journal of Biological Chemistry, 280(52), 42685–42693. doi:10.1074/jbc.M510042200
   PubMed Web of Science ®Google Scholar
• Narumi, T., Yasuoka, K., Taiji, M., & Hofinger, S. (2009). Current performance gains from utilizing the GPU or the ASIC MDGRAPE-3 within an enhanced Poisson Boltzmann approach. Journal of Computational Chemistry, 30(14), 2351–2357. doi:10.1002/jcc.21257
   PubMed Web of Science ®Google Scholar
• Pastor, R. W., Brooks, B. R., & Szabo, A. (1988). An analysis of the accuracy of Langevin and molecular dynamics algorithms. Molecular Physics, 65(6), 1409–1419. doi:10.1080/00268978800101881
   Web of Science ®Google Scholar
• Piala, A. T., Moon, T. M., Akella, R., He, H., Cobb, M. H., & Goldsmith, E. J. (2014). Chloride sensing by WNK1 involves inhibition of autophosphorylation. Science Signaling, 7(324), ra41. doi:10.1126/scisignal.2005050
   PubMed Web of Science ®Google Scholar
• Piton, A., Gauthier, J., Hamdan, F., Lafreniere, R., Yang, Y., Henrion, E., … Karemera, L. (2011). Systematic resequencing of X-chromosome synaptic genes in autism spectrum disorder and schizophrenia. Molecular Psychiatry, 16(8), 867. doi:10.1038/mp.2010.54
   PubMed Web of Science ®Google Scholar
• Rempe, S. B., & Jónsson, H. (1998). A computational exercise illustrating molecular vibrations and normal modes. The Chemical Educator, 3(4), 1–17. doi:10.1007/s00897980231a
   Google Scholar
• Righino, B., Galisson, F., Pirolli, D., Vitale, S., Réty, S., Gouet, P., & De Rosa, M. C. (2018). Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments. Journal of Biomolecular Structure and Dynamics, 36(14), 3666–3679. doi:10.1080/07391102.2017.1395767
   PubMed Web of Science ®Google Scholar
• Rinehart, J., Kahle, K. T., de los Heros, P., Vazquez, N., Meade, P., Wilson, F. H., … Lifton, R. P. (2005). WNK3 kinase is a positive regulator of NKCC2 and NCC, renal cation-Cl-cotransporters required for normal blood pressure homeostasis. Proceedings of the National Academy of Sciences USA, 102(46), 16777–16782. doi:10.1073/pnas.0508303102
   PubMed Web of Science ®Google Scholar
• Shahbaaz, M., Kanchi, S., Sabela, M., & Bisetty, K. (2018). Structural basis of pesticide detection by enzymatic biosensing: a molecular docking and MD simulation study. Journal of Biomolecular Structure and Dynamics, 36(6), 1402–1416. doi:10.1080/07391102.2017.1323673
   PubMed Web of Science ®Google Scholar
• Sievers, F., Wilm, A., Dineen, D., Gibson, T. J., Karplus, K., Li, W., … Söding, J. (2011). Fast, scalable generation of high‐quality protein multiple sequence alignments using Clustal Omega. Molecular Systems Biology, 7(1), 539. doi:10.1038/msb.2011.75
   PubMed Web of Science ®Google Scholar
• Sithanandam, G., Kolch, W., Duh, F., & Rapp, U. (1990). Complete coding sequence of a human B-raf cDNA and detection of B-raf protein kinase with isozyme specific antibodies. Oncogene, 5, 1775–1780.
   PubMed Web of Science ®Google Scholar
• Srivastava, H. K., & Sastry, G. N. (2012). Molecular dynamics investigation on a series of HIV protease inhibitors: assessing the performance of MM-PBSA and MM-GBSA approaches. Journal of Chemical Information and Modeling, 52(11), 3088–3098. doi:10.1021/ci300385h
   PubMed Web of Science ®Google Scholar
• Suplatov, D., Kopylov, K., Sharapova, Y., & Švedas, V. (2018). Human p38α Mitogen-Activated Protein Kinase in the Asp168-Phe169-Gly170-in (DFG-in) state can bind allosteric inhibitor Doramapimod. Journal of Biomolecular Structure and Dynamics, (in press). doi:10.1080/07391102.2018.1475260
   PubMed Web of Science ®Google Scholar
• Veríssimo, F., & Jordan, P. (2001). WNK kinases, a novel protein kinase subfamily in multi-cellular organisms. Oncogene, 20, 5562–5569.
   PubMed Web of Science ®Google Scholar
• Verissimo, F., Silva, E., Morris, J., Pepperkok, R., & Jordan, P. (2006). Protein kinase WNK3 increases cell survival in a caspase-3-dependent pathway. Oncogene, 25(30), 4172–4178. doi:10.1038/sj.onc.1209449
   Web of Science ®Google Scholar
• Vitari, A. C., Deak, M., Morrice, N. A., & Alessi, D. R. (2005). The WNK1 and WNK4 protein kinases that are mutated in Gordon's hypertension syndrome phosphorylate and activate SPAK and OSR1 protein kinases. Biochemical Journal, 391(1), 17–24. doi:10.1042/BJ20051180
   PubMedGoogle Scholar
• Wallace, A. C., Laskowski, R. A., & Thornton, J. M. (1995). LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Engineering, Design and Selection, 8(2), 127–134. doi:10.1093/protein/8.2.127
   Web of Science ®Google Scholar
• Wang, J., Wang, W., Kollman, P. A., & Case, D. A. (2006). Automatic atom type and bond type perception in molecular mechanical calculations. Journal of Molecular Graphics Modelling, 25(2), 247–260. doi:10.1016/j.jmgm.2005.12.005
   PubMed Web of Science ®Google Scholar
• Wang, J., Wolf, R. M., Caldwell, J. W., Kollman, P. A., & Case, D. A. (2004). Development and testing of a general amber force field. Journal of Computational Chemistry, 25(9), 1157–1174. doi:10.1002/jcc.20035
   PubMed Web of Science ®Google Scholar
• Wang, Z., Liu, J., Sudom, A., Ayres, M., Li, S., Wesche, H., … Walker, N. P. (2006). Crystal structures of IRAK-4 kinase in complex with inhibitors: a serine/threonine kinase with tyrosine as a gatekeeper. Structure, 14, 1835–1844. doi:10.1016/j.str.2006.11.001
   PubMed Web of Science ®Google Scholar
• Weiser, J., Shenkin, P. S., & Still, W. C. (1999). Fast, approximate algorithm for detection of solvent‐inaccessible atoms. Journal of Computational Chemistry, 20(6), 586–596. doi:10.1002/(SICI)1096-987X(19990430)20:6<586::AID-JCC4>3.0.CO;2-J
   Web of Science ®Google Scholar
• Wilson, F. H., Disse-Nicodeme, S., Choate, K. A., Ishikawa, K., Nelson-Williams, C., Desitter, I., … Achard, J.-M. (2001). Human hypertension caused by mutations in WNK kinases. Science, 293, 1107–1112.
   Google Scholar
• Worch, R., Bokel, C., Hofinger, S., Schwille, P., & Weidemann, T. (2010). Focus on composition and interaction potential of single-pass transmembrane domains. PROTEOMICS, 10(23), 4196–4208. doi:10.1002/pmic.201000208
   PubMed Web of Science ®Google Scholar
• Wu, S., & Zhang, Y. (2007). LOMETS: a local meta-threading-server for protein structure prediction. Nucleic Acids Research, 35(10), 3375–3382. doi:10.1093/nar/gkm251
   PubMed Web of Science ®Google Scholar
• Xu, B-e., English, J. M., Wilsbacher, J. L., Stippec, S., Goldsmith, E. J., & Cobb, M. H. (2000). WNK1, a novel mammalian serine/threonine protein kinase lacking the catalytic lysine in subdomain II. Journal of Biological Chemistry, 275(22), 16795–16801. doi:10.1074/jbc.275.22.16795
   PubMed Web of Science ®Google Scholar
• Xu, BE., Min, X., Stippec, S., Lee, B.-H., Goldsmith, E. J., & Cobb, M. H. (2002). Regulation of WNK1 by an autoinhibitory domain and autophosphorylation. Journal of Biological Chemistry, 277(50), 48456–48462. doi:10.1074/jbc.M207917200
   PubMed Web of Science ®Google Scholar
• Xu, BE, Stippec, S., Lenertz, L., Lee, B.-H., Zhang, W., Lee, Y.-K., & Cobb, M. H. (2004). WNK1 activates ERK5 by an MEKK2/3-dependent mechanism. Journal of Biological Chemistry, 279(9), 7826–7831. doi:10.1074/jbc.M313465200
   PubMed Web of Science ®Google Scholar
• Yamada, K., Park, H.-M., Rigel, D. F., DiPetrillo, K., Whalen, E. J., Anisowicz, A., … Burdick, D. A. (2016). Small-molecule WNK inhibition regulates cardiovascular and renal function. Nature Chemical Biology, 12(11), 896. doi:10.1038/nchembio.2168
   PubMed Web of Science ®Google Scholar
• Yan, F., Liu, X., Zhang, S., Su, J., Zhang, Q., & Chen, J. (2018). Computational revelation of binding mechanisms of inhibitors to endocellular protein tyrosine phosphatase 1B using molecular dynamics simulations. Journal of Biomolecular Structure and Dynamics, 36(14), 3636–3650. doi:10.1080/07391102.2017.1394221
   PubMed Web of Science ®Google Scholar
• Yu, Y., Wang, J., Shao, Q., Shi, J., & Zhu, W. (2015). Effects of drug-resistant mutations on the dynamic properties of HIV-1 protease and inhibition by Amprenavir and Darunavir. Scientific Reports, 5, 10517. doi:10.1038/srep10517
   PubMed Web of Science ®Google Scholar
• Zhang, Y. (2008). I-TASSER server for protein 3D structure prediction. BMC Bioinformatics, 9, 40. doi:10.1186/1471-2105-9-40
   PubMed Web of Science ®Google Scholar
• Zwanzig, R. W. (1954). High‐temperature equation of state by a perturbation method. I. Nonpolar gases. The Journal of Chemical Physics, 22(8), 1420–1426. doi:10.1063/1.1740409
   Web of Science ®Google Scholar