Research article

Heat conduction by thyroid hormone receptors

  • Received: 10 August 2018 Accepted: 16 October 2018 Published: 25 October 2018
  • Thyroid hormone receptors (THRs) together with hormone binding and dissociation are important in gene expressions. The heat conduction properties such as heat capacity, thermal diffusivity and thermal conductivity of THR isoforms are determined by means of molecular dynamics simulations. Mean energy fluctuations in canonical ensemble at 310 K and theory of mole fraction are used to find the heat capacity of THRs in solution. The larger heat capacity of liganded THR-β than that of unliganded THR-β signifies the effect of receptor-ligand interactions, and hydrophobic, vibrational and conformational changes. The specific heats of THR isoforms in solution range from 2000 to 2200 Jkg−1K−1 at 310 K which lie within the experimental range for the native globular proteins. Providing temperature relaxation from 310 K to 200 K across protein-water interface in nano-droplets, the thermal diffusivity of THRs ranges from 1.28×10−7 to 1.57×10−7 m2/s which is around 1.46×10−7 m2/s for water. The thermal conductivity of THRs lies in the range 0.26–0.30 Wm−1K1 which is about half the value, 0.64 Wm−1K1 for water at 310 K.

    Citation: Tika Ram Lamichhane, Hari Prasad Lamichhane. Heat conduction by thyroid hormone receptors[J]. AIMS Biophysics, 2018, 5(4): 245-256. doi: 10.3934/biophy.2018.4.245

    Related Papers:

  • Thyroid hormone receptors (THRs) together with hormone binding and dissociation are important in gene expressions. The heat conduction properties such as heat capacity, thermal diffusivity and thermal conductivity of THR isoforms are determined by means of molecular dynamics simulations. Mean energy fluctuations in canonical ensemble at 310 K and theory of mole fraction are used to find the heat capacity of THRs in solution. The larger heat capacity of liganded THR-β than that of unliganded THR-β signifies the effect of receptor-ligand interactions, and hydrophobic, vibrational and conformational changes. The specific heats of THR isoforms in solution range from 2000 to 2200 Jkg−1K−1 at 310 K which lie within the experimental range for the native globular proteins. Providing temperature relaxation from 310 K to 200 K across protein-water interface in nano-droplets, the thermal diffusivity of THRs ranges from 1.28×10−7 to 1.57×10−7 m2/s which is around 1.46×10−7 m2/s for water. The thermal conductivity of THRs lies in the range 0.26–0.30 Wm−1K1 which is about half the value, 0.64 Wm−1K1 for water at 310 K.


    加载中
    [1] Brent GA (2012) Mechanisms of thyroid hormone action. J Clin Invest 122: 3035–3043. doi: 10.1172/JCI60047
    [2] Souza PCT, Puhl AC, Martínez L, et al. (2014) Identification of a new hormone-binding site on the surface of thyroid hormone receptor. Mol Endocrinol 28: 534–545. doi: 10.1210/me.2013-1359
    [3] Bochukova E, Schoenmakers N, Agostini M, et al. (2012) A mutation in the thyroid hormone receptor alpha gene. New Eng J Med 366: 243–249. doi: 10.1056/NEJMoa1110296
    [4] Brent GA (1994) The molecular basis of thyroid hormone action. Eng J Med 331: 847–853. doi: 10.1056/NEJM199409293311306
    [5] Leitner DM (2008) Energy flow in proteins. Annu Rev Phys Chem 59: 233–259.
    [6] Prabhu NV, Sharp KA (2005) Heat capacity in proteins. Annu Rev Phys Chem 56: 521–548. doi: 10.1146/annurev.physchem.56.092503.141202
    [7] Privalov PL, Tiktopulo EI, Venyaminov SY, et al. (1989) Heat capacity and conformation of proteins in the denatured state. J Mol Biol 205: 737–750. doi: 10.1016/0022-2836(89)90318-5
    [8] Yu X, Leitner DM (2005) Heat flow in proteins: Computation of thermal transport coefficients. J Chem Phys 122: 054902. doi: 10.1063/1.1830431
    [9] Lervik A, Bresme F, Kjelstrup S, et al. (2010) Heat transfer in protein-water interfaces. Phys Chem Chem Phys 12: 1610–1617. doi: 10.1039/b918607g
    [10] Helbing J, Devereux M, Nienhaus K, et al. (2011) Temperature dependence of the heat diffusivity of proteins. J Phys Chem A 116: 2620–2628.
    [11] Nosé S (1984) A molecular dynamics method for simulations in the canonical ensemble. Mol Phys 52: 255–268. doi: 10.1080/00268978400101201
    [12] Suurkuusk J (1974) Specific heat measurements on lysozyme, chymotrypsinogen, and ovalbumin in aqueous solution and in solid state. Acta Chem Scand B 28: 409–417.
    [13] Yang PH, Rupley JA (1979) Protein-water interactions. Heat capacity of the lysozyme-water system. Biochemistry 18: 2654–2661.
    [14] Lervik A, Bresme F, Kjelstrup S (2009) Heat transfer in soft nanoscale interfaces: The influence of interface curvature. Soft Matter 5: 2407–2414. doi: 10.1039/b817666c
    [15] Nascimento AS, Dia SMG, Nunes FM, et al. (2006) Structural rearrangements in the thyroid hormone receptor hinge domain and their putative role in the receptor function. J Mol Biol 360: 586–598. doi: 10.1016/j.jmb.2006.05.008
    [16] Sandler B, Webb P, Apriletti JW, et al. (2004) Thyroxine-thyroid hormone receptor interactions. J Biol Chem 279: 55801–55808. doi: 10.1074/jbc.M410124200
    [17] Souza PCT, Puhl AC, Martínez L, et al. (2014) Identification of a new hormone-binding site on the surface of thyroid hormone receptor. Mol Endocrinol 28: 534–545. doi: 10.1210/me.2013-1359
    [18] Mackerell AD, Feig M, Brooks CL (2004) Extending the treatment of backbone energetics in protein force fields: Limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations. J Comp Chem 25: 1400–1415.
    [19] Mackerell JAD, Bashford D, Bellott MLDR, et al. (1998) All-atom empirical potential for molecular modeling and dynamics studies of proteins. J Phys Chem B 102: 3586–3616. doi: 10.1021/jp973084f
    [20] Zoete V, Cuendet MA, Grosdidier A, et al. (2011) SwissParam: A fast force field generation tool for small organic molecules. J Comp Chem 32: 2359–2368. doi: 10.1002/jcc.21816
    [21] Humphrey W, Dalke A, Schulten K (1996) VMD: Visual molecular dynamics. J Mol Graph 14: 33–38. doi: 10.1016/0263-7855(96)00018-5
    [22] Phillips JC, Braun R, Wang W, et al. (2005) Scalable molecular dynamics with NAMD. J Comp Chem 26: 1781–1802.
    [23] Eftink MR, Anusiem AC, Biltonen RL (1983) Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A. Biochemistry 22: 3884–3896. doi: 10.1021/bi00285a025
    [24] Sturtevant JM (1977) Heat capacity and entropy changes in processes involving proteins. Proc Natl Acad Sci 74: 2236–2240. doi: 10.1073/pnas.74.6.2236
    [25] Privalov PL, Potekhin SA (1986) Scanning microcalorimetry in studying temperature-induced changes in proteins. Method enzymol 131: 4–51. doi: 10.1016/0076-6879(86)31033-4
    [26] Privalov PL, Dragan AI (2007) Microcalorimetry of biological macromolecules. Biophys Chem 126: 16–24.
    [27] Gomez J, Hilser VJ, Xie D, et al. (1995) The heat capacity of proteins. Proteins: Struct, Funct, Bioinf 22: 404–412. doi: 10.1002/prot.340220410
    [28] Cooper A (2000) Heat capacity of hydrogen-bonded networks: An alternative view of protein folding thermodynamics. Biophys Chem 85: 25–39. doi: 10.1016/S0301-4622(00)00136-8
    [29] Pandey HD, Leitner DM (2017) Thermodynamics of hydration water around an antifreeze protein: A molecular simulation study. J Phys Chem B 121: 9498–9507. doi: 10.1021/acs.jpcb.7b05892
    [30] Xu Y, Leitner DM (2014) Vibrational energy flow through the green fluorescent protein-water interface: Communication maps and thermal boundary conductance. J Phys Chem B 118: 7818–7826.
  • Reader Comments
  • © 2018 the Author(s), licensee AIMS Press. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0)
通讯作者: 陈斌, bchen63@163.com
  • 1. 

    沈阳化工大学材料科学与工程学院 沈阳 110142

  1. 本站搜索
  2. 百度学术搜索
  3. 万方数据库搜索
  4. CNKI搜索

Metrics

Article views(4336) PDF downloads(1822) Cited by(4)

Article outline

Figures and Tables

Figures(5)  /  Tables(2)

Other Articles By Authors

/

DownLoad:  Full-Size Img  PowerPoint
Return
Return

Catalog