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The kinetic mechanism of H+ in lysozyme with increasing temperature

  • Department of Chemical Physics, University of Science and Technology of China, Hefei 230026, China

Cite this:
https://doi.org/10.3969/j.issn.0253-2778.2020.05.011
  • Received Date: 26 April 2019
  • Accepted Date: 31 May 2019
  • Rev Recd Date: 31 May 2019
  • Publish Date: 31 May 2020
    Abstract

  • Abstract

    In this study, Raman spectroscopy was employed to study the kinetic mechanism of lysozyme denaturation at high temperatures induced by

    Abstract

    In this study, Raman spectroscopy was employed to study the kinetic mechanism of lysozyme denaturation at high temperatures induced by
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    • References(42)
  • [1]
    DOBSON C M. Protein folding and misfolding[J]. Nature, 2003, 426(6968): 884-890.
    [2]
    NEUDECKER P, ROBUSTELLI P, CAVALLI A, et al. Structure of an intermediate state in protein folding and aggregation[J]. Science, 2012, 336(6079): 362-366.
    [3]
    CAMPBELL L, RAIKOS V, EUSTON S R. Modification of functional properties of egg-white proteins[J]. Nahrung, 2003, 47(6): 369-376.
    [4]
    HANDA A, TAKAHASHI K, KURODA N, et al. Heat-induced egg white gels as affected by pH[J]. Journal of Food Science, 1998, 63(3): 403-407.
    [5]
    MINE Y, NOUTOMI T, HAGA N. Thermally induced changes in egg-white proteins[J]. J Agr Food Chem, 1990, 38(12): 2122-2125.
    [6]
    DU H B, LIU Z Z, JENNINGS R, et al. The effects of salt ions on the dynamics and thermodynamics of lysozyme unfolding[J]. Sep Sci Technol, 2017, 52(2): 320-331.
    [7]
    谢栒, 周平, 邓风, 等. pH 值对丝素蛋白构象转变的影响[J]. 高等学校化学学报, 2004, 25(5): 961-965.
    [8]
    CANFIELD R E. Amino acid sequence of egg white lysozyme[J]. J Biol Chem, 1963, 238(8): 2698-2708.
    [9]
    VANEY M C, MAIGNAN S, RIES-KAUTT M, et al. High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission[J]. Acta Crystallogr D Biol Crystallogr, 1996, 52: 505-517.
    [10]
    WANG S S, CHAO H S, LIU H L, et al. Stability of hen egg white lysozyme during denaturation is enhanced by pretreatment with supercritical carbon dioxide[J]. J Biosci Bioeng, 2009, 107(4): 355-359.
    [11]
    VENKATARAMANI S, TRUNTZER J, COLEMAN D R. Thermal stability of high concentration lysozyme across varying pH: A Fourier transform infrared study[J]. J Pharm Bioallied Sci, 2013, 5(2): 148-153.
    [12]
    XING L, LIN K, ZHOU X G, et al. Multistate mechanism of lysozyme denaturation through synchronous analysis of Raman spectra[J]. J Phys Chem B, 2016, 120(41): 10660-10667.
    [13]
    BARRECA D, LAGANA G, MAGAZU S, et al. FTIR, ESI-MS, VT-NMR and SANS study of trehalose thermal stabilization of lysozyme[J]. Int J Biol Macromol, 2014, 63(225-32.
    [14]
    HIRAI M, ARAI S, IWASE H. Complementary analysis of thermal transition multiplicity of hen egg-white lysozyme at low pH using X-ray scattering and scanning calorimetry[J]. J Phys Chem B, 1999, 103(3): 549-556.
    [15]
    XING L, FAN W, CHEN N, et al. Amyloid formation kinetics of hen egg white lysozyme under heat and acidic conditions revealed by Raman spectroscopy[J]. J Raman Spectrosc, 201950(5): 629-640.,
    [16]
    XING L, CHEN N, FAN W, et al. Double-edged effects of aluminium ions on amyloid fibrillation of hen egg-white lysozyme[J]. Int J Biol Macromol, 2019,132: 929-938.
    [17]
    LEWIS E N, QI W, KIDDER L H, et al. Combined dynamic light scattering and Raman spectroscopy approach for characterizing the aggregation of therapeutic proteins[J]. Molecules, 2014, 19(12): 20888-20905.
    [18]
    CHEN L, ZHU W D, LIN K, et al. Identification of alcohol conformers by Raman spectra in the C-H stretching region[J]. J Phys Chem A, 2015, 119(13): 3209-3217.
    [19]
    LIN K, HU N Y, ZHOU X G, et al. Reorientation dynamics in liquid alcohols from Raman spectroscopy[J]. J Raman Spectrosc, 2012, 43(1): 82-88.
    [20]
    LIN K, ZHOU X G, LIU S L, et al. Identification of free OH and its implication on structural changes of liquid water[J]. Chinese J Chem Phys, 2013, 26(2): 121-126.
    [21]
    LIN K, ZHOU X G, LUO Y, et al. The microscopic structure of liquid methanol from Raman spectroscopy[J]. J Phys Chem B, 2010, 114(10): 3567-3573.
    [22]
    TANG C Q, LIN K, ZHOU X G, et al. In situ detection of amide a bands of proteins in water by Raman spectrum[J]. Chinese J Chem Phys, 2016, 29(1): 129-134.
    [23]
    WANG C C, LIN K, HU N Y, et al. Ion pairs in aqueous magnesium nitrate solution by excess Raman spectroscopy[J]. Acta Phys-Chim Sin, 2012, 28(8): 1823-1829.
    [24]
    ELWELL M L, SCHELLMAN J A. Stability of phage-T4 lysozymes.1. Native properties and thermal-stability of wild-type and 2 mutant lysozymes[J]. Biochim Biophys Acta, 1977, 494(2): 367-383.
    [25]
    HEDOUX A, IONOV R, WILLART J F, et al. Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation[J]. J Chem Phys, 2006, 124(1):1604.
    [26]
    THOMSON J A, SHIRLEY B A, GRIMSLEY G R, et al. Conformational stability and mechanism of folding of ribonuclease-T1[J]. J Biol Chem, 1989, 264(20): 11614-11620.
    [27]
    VANSTOKKUM I H M, SCHERER T, BROUWER A M, et al. Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parameterization of fluorescence[J]. J Phys Chem-Us, 1994, 98(3): 852-866.
    [28]
    CHEN M C, LORD R C, MENDELSOHN R. Laser-excited Raman-spectroscopy of biomolecules.5. Conformational-changes associated with chemical denaturation of lysozyme[J]. J Am Chem Soc, 1974, 96(10): 3038-3042.
    [29]
    ELLIS D I, COWCHER D P, ASHTON L, et al. Illuminating disease and enlightening biomedicine: Raman spectroscopy as a diagnostic tool[J]. Analyst, 2013, 138(14): 3871-3884.
    [30]
    KOCHERBITOV V, LATYNIS J, MISIUNAS A, et al. Hydration of lysozyme studied by Raman spectroscopy[J]. J Phys Chem B, 2013, 117(17): 4981-4992.
    [31]
    LORD R C, YU N T. Laser-Excited Raman spectroscopy of biomolecules.2. Native ribonucuease and alpha-chymotrypsin[J]. J Mol Biol, 1970, 51(2):203-213.
    [32]
    LORD R C, YU N T. Laser-Excited Raman spectroscopy of biomolecules.1. Native lysozyme and its constituent amino acids[J]. J Mol Biol, 1970, 50(2):509-524.
    [33]
    RYGULA A, MAJZNER K, MARZEC K M, et al. Raman spectroscopy of proteins: a review[J]. J Raman Spectrosc, 2013, 44(8): 1061-1076.
    [34]
    SIAMWIZA M N, LORD R C, CHEN M C, et al. Interpretation of doublet at 850 and 830 Cm-1 in Raman-spectra of tyrosyl residues in proteins and certain model compounds[J]. Biochemistry-Us, 1975, 14(22): 4870-4876.
    [35]
    SPIRO T G, GABER B P. Laser Raman-scattering as a probe of protein-structure[J]. Annu Rev Biochem, 1977, 46(1):553-572.
    [36]
    SWEENEY J A, ASHER S A. Tryptophan UV resonance Raman excitation profiles[J]. J Phys Chem, 1990, 94(12): 4784-4791.
    [37]
    WEN Z Q. Raman spectroscopy of protein pharmaceuticals[J]. J Pharm Sci, 2007, 96(11): 2861-2878.
    [38]
    SEO J A, HEDOUX A, GUINET Y, et al. Thermal denaturation of beta-lactoglobulin and stabilization mechanism by trehalose analyzed from Raman spectroscopy investigations[J]. J Phys Chem B, 2010, 114(19): 6675-6684.
    [39]
    TORREGGIANI A, DI FOGGIA M, MANCO I, et al. Effect of sulfoxides on the thermal denaturation of hen lysozyme: A calorimetric and Raman study[J]. J Mol Struct, 2008, 891(1-3): 115-122.
    [40]
    TAKEUCHI H. Raman structural markers of tryptophan and histidine side chains in proteins[J]. Biopolymers, 2003, 72(5): 305-317.
    [41]
    TAKEUCHI H. UV Raman markers for structural analysis of aromatic side chains in proteins[J]. Anal Sci, 2011, 27(11): 1077-1086.
    [42]
    CHEN M C, LORD R C, MENDELSOHN R. Laser-excited Raman-spectroscopy of biomolecules.4. Thermal denaturation of aqueous lysozyme[J]. Biochim Biophys Acta, 1973, 328(2): 252-260.)
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    [1]
    DOBSON C M. Protein folding and misfolding[J]. Nature, 2003, 426(6968): 884-890.
    [2]
    NEUDECKER P, ROBUSTELLI P, CAVALLI A, et al. Structure of an intermediate state in protein folding and aggregation[J]. Science, 2012, 336(6079): 362-366.
    [3]
    CAMPBELL L, RAIKOS V, EUSTON S R. Modification of functional properties of egg-white proteins[J]. Nahrung, 2003, 47(6): 369-376.
    [4]
    HANDA A, TAKAHASHI K, KURODA N, et al. Heat-induced egg white gels as affected by pH[J]. Journal of Food Science, 1998, 63(3): 403-407.
    [5]
    MINE Y, NOUTOMI T, HAGA N. Thermally induced changes in egg-white proteins[J]. J Agr Food Chem, 1990, 38(12): 2122-2125.
    [6]
    DU H B, LIU Z Z, JENNINGS R, et al. The effects of salt ions on the dynamics and thermodynamics of lysozyme unfolding[J]. Sep Sci Technol, 2017, 52(2): 320-331.
    [7]
    谢栒, 周平, 邓风, 等. pH 值对丝素蛋白构象转变的影响[J]. 高等学校化学学报, 2004, 25(5): 961-965.
    [8]
    CANFIELD R E. Amino acid sequence of egg white lysozyme[J]. J Biol Chem, 1963, 238(8): 2698-2708.
    [9]
    VANEY M C, MAIGNAN S, RIES-KAUTT M, et al. High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission[J]. Acta Crystallogr D Biol Crystallogr, 1996, 52: 505-517.
    [10]
    WANG S S, CHAO H S, LIU H L, et al. Stability of hen egg white lysozyme during denaturation is enhanced by pretreatment with supercritical carbon dioxide[J]. J Biosci Bioeng, 2009, 107(4): 355-359.
    [11]
    VENKATARAMANI S, TRUNTZER J, COLEMAN D R. Thermal stability of high concentration lysozyme across varying pH: A Fourier transform infrared study[J]. J Pharm Bioallied Sci, 2013, 5(2): 148-153.
    [12]
    XING L, LIN K, ZHOU X G, et al. Multistate mechanism of lysozyme denaturation through synchronous analysis of Raman spectra[J]. J Phys Chem B, 2016, 120(41): 10660-10667.
    [13]
    BARRECA D, LAGANA G, MAGAZU S, et al. FTIR, ESI-MS, VT-NMR and SANS study of trehalose thermal stabilization of lysozyme[J]. Int J Biol Macromol, 2014, 63(225-32.
    [14]
    HIRAI M, ARAI S, IWASE H. Complementary analysis of thermal transition multiplicity of hen egg-white lysozyme at low pH using X-ray scattering and scanning calorimetry[J]. J Phys Chem B, 1999, 103(3): 549-556.
    [15]
    XING L, FAN W, CHEN N, et al. Amyloid formation kinetics of hen egg white lysozyme under heat and acidic conditions revealed by Raman spectroscopy[J]. J Raman Spectrosc, 201950(5): 629-640.,
    [16]
    XING L, CHEN N, FAN W, et al. Double-edged effects of aluminium ions on amyloid fibrillation of hen egg-white lysozyme[J]. Int J Biol Macromol, 2019,132: 929-938.
    [17]
    LEWIS E N, QI W, KIDDER L H, et al. Combined dynamic light scattering and Raman spectroscopy approach for characterizing the aggregation of therapeutic proteins[J]. Molecules, 2014, 19(12): 20888-20905.
    [18]
    CHEN L, ZHU W D, LIN K, et al. Identification of alcohol conformers by Raman spectra in the C-H stretching region[J]. J Phys Chem A, 2015, 119(13): 3209-3217.
    [19]
    LIN K, HU N Y, ZHOU X G, et al. Reorientation dynamics in liquid alcohols from Raman spectroscopy[J]. J Raman Spectrosc, 2012, 43(1): 82-88.
    [20]
    LIN K, ZHOU X G, LIU S L, et al. Identification of free OH and its implication on structural changes of liquid water[J]. Chinese J Chem Phys, 2013, 26(2): 121-126.
    [21]
    LIN K, ZHOU X G, LUO Y, et al. The microscopic structure of liquid methanol from Raman spectroscopy[J]. J Phys Chem B, 2010, 114(10): 3567-3573.
    [22]
    TANG C Q, LIN K, ZHOU X G, et al. In situ detection of amide a bands of proteins in water by Raman spectrum[J]. Chinese J Chem Phys, 2016, 29(1): 129-134.
    [23]
    WANG C C, LIN K, HU N Y, et al. Ion pairs in aqueous magnesium nitrate solution by excess Raman spectroscopy[J]. Acta Phys-Chim Sin, 2012, 28(8): 1823-1829.
    [24]
    ELWELL M L, SCHELLMAN J A. Stability of phage-T4 lysozymes.1. Native properties and thermal-stability of wild-type and 2 mutant lysozymes[J]. Biochim Biophys Acta, 1977, 494(2): 367-383.
    [25]
    HEDOUX A, IONOV R, WILLART J F, et al. Evidence of a two-stage thermal denaturation process in lysozyme: A Raman scattering and differential scanning calorimetry investigation[J]. J Chem Phys, 2006, 124(1):1604.
    [26]
    THOMSON J A, SHIRLEY B A, GRIMSLEY G R, et al. Conformational stability and mechanism of folding of ribonuclease-T1[J]. J Biol Chem, 1989, 264(20): 11614-11620.
    [27]
    VANSTOKKUM I H M, SCHERER T, BROUWER A M, et al. Conformational dynamics of flexibly and semirigidly bridged electron donor-acceptor systems as revealed by spectrotemporal parameterization of fluorescence[J]. J Phys Chem-Us, 1994, 98(3): 852-866.
    [28]
    CHEN M C, LORD R C, MENDELSOHN R. Laser-excited Raman-spectroscopy of biomolecules.5. Conformational-changes associated with chemical denaturation of lysozyme[J]. J Am Chem Soc, 1974, 96(10): 3038-3042.
    [29]
    ELLIS D I, COWCHER D P, ASHTON L, et al. Illuminating disease and enlightening biomedicine: Raman spectroscopy as a diagnostic tool[J]. Analyst, 2013, 138(14): 3871-3884.
    [30]
    KOCHERBITOV V, LATYNIS J, MISIUNAS A, et al. Hydration of lysozyme studied by Raman spectroscopy[J]. J Phys Chem B, 2013, 117(17): 4981-4992.
    [31]
    LORD R C, YU N T. Laser-Excited Raman spectroscopy of biomolecules.2. Native ribonucuease and alpha-chymotrypsin[J]. J Mol Biol, 1970, 51(2):203-213.
    [32]
    LORD R C, YU N T. Laser-Excited Raman spectroscopy of biomolecules.1. Native lysozyme and its constituent amino acids[J]. J Mol Biol, 1970, 50(2):509-524.
    [33]
    RYGULA A, MAJZNER K, MARZEC K M, et al. Raman spectroscopy of proteins: a review[J]. J Raman Spectrosc, 2013, 44(8): 1061-1076.
    [34]
    SIAMWIZA M N, LORD R C, CHEN M C, et al. Interpretation of doublet at 850 and 830 Cm-1 in Raman-spectra of tyrosyl residues in proteins and certain model compounds[J]. Biochemistry-Us, 1975, 14(22): 4870-4876.
    [35]
    SPIRO T G, GABER B P. Laser Raman-scattering as a probe of protein-structure[J]. Annu Rev Biochem, 1977, 46(1):553-572.
    [36]
    SWEENEY J A, ASHER S A. Tryptophan UV resonance Raman excitation profiles[J]. J Phys Chem, 1990, 94(12): 4784-4791.
    [37]
    WEN Z Q. Raman spectroscopy of protein pharmaceuticals[J]. J Pharm Sci, 2007, 96(11): 2861-2878.
    [38]
    SEO J A, HEDOUX A, GUINET Y, et al. Thermal denaturation of beta-lactoglobulin and stabilization mechanism by trehalose analyzed from Raman spectroscopy investigations[J]. J Phys Chem B, 2010, 114(19): 6675-6684.
    [39]
    TORREGGIANI A, DI FOGGIA M, MANCO I, et al. Effect of sulfoxides on the thermal denaturation of hen lysozyme: A calorimetric and Raman study[J]. J Mol Struct, 2008, 891(1-3): 115-122.
    [40]
    TAKEUCHI H. Raman structural markers of tryptophan and histidine side chains in proteins[J]. Biopolymers, 2003, 72(5): 305-317.
    [41]
    TAKEUCHI H. UV Raman markers for structural analysis of aromatic side chains in proteins[J]. Anal Sci, 2011, 27(11): 1077-1086.
    [42]
    CHEN M C, LORD R C, MENDELSOHN R. Laser-excited Raman-spectroscopy of biomolecules.4. Thermal denaturation of aqueous lysozyme[J]. Biochim Biophys Acta, 1973, 328(2): 252-260.)
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