Exposure of thiol groups in the heat-induced denaturation of β-lactoglobulin

Molecular Simulation

Volumn 41, Issue 10-12, 2015, Pages 1006-1014

  Zeiler, Rosanne N W ^a   Bolhuis, Peter G ^a  

^a UNIVERSITY OF AMSTERDAM   (Netherlands)

Author keywords

aggregation; proteins; replica exchange molecular dynamics

Indexed keywords

AGGLOMERATION; AMINO ACIDS; GELATION; PROTEINS; SULFUR COMPOUNDS;

BETA-LACTOGLOBULIN; DISULPHIDE BRIDGE; DISULPHIDE EXCHANGE; EXPOSURE MECHANISM; MOLECULAR MECHANISM; PROTEIN AGGREGATES; REPLICA EXCHANGE MOLECULAR DYNAMICS; REPLICA-EXCHANGE MOLECULAR DYNAMICS SIMULATIONS;

MOLECULAR DYNAMICS;

EID: 84931003985     PISSN: 08927022     EISSN: 10290435     Source Type: Journal    
DOI: 10.1080/08927022.2014.926547     Document Type: Conference Paper

References (30)

1. Bryant CM, McClements DJ. Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey. Trends Food Sci Technol. 1998; 9: 143-151.
2. Witde JN. Thermal behaviour of bovine beta-lactoglobulin at temperatures up to 150°C: a review. Trends Food Sci Technol. 2009; 20: 27-34.
3. Floris R, Bodnár I, Weinbreck F, Alting AC. Dynamic rearrangement of disulfide bridges influences solubility of whey protein coatings. Int Dairy J. 2008; 18: 566-573.
4. Hoffmann MAM, Milvan PJJM. Heat-induced aggregation of beta-lactoglobulin: role of the free thiol group and disulfide bonds. J Agric Food Chem. 1997; 45: 2942-2948.
5. Sakurai K, Konuma T, Yagi M, Goto Y. Structural dynamics and folding of beta-lactoglobulin probed by heteronuclear NMR. Biochim Biophys Acta Gen Subj. 2009; 1790: 527-537.
6. Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson B. Structural basis of the tanford transition of bovine beta-lactoglobulin. Biochemistry. 1998; 37: 14014-14023.
7. Relkin P. Thermal unfolding of beta-lactoglobulin, alpha-lactalbumin, and bovine serum albumin: a thermodynamic approach. Crit Rev Food Sci Nutr. 1996; 36: 565-601.
8. Qi XL, Holt C, McNulty D, Clarke DT, Brownlow S, Jones GR. Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem J. 1997; 324: 341-346.
9. Livney YD, Verespej E, Dalgleish DG. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of beta-lactoglobulin B and alpha-lactalbumin. J Agric Food Chem. 2003; 51: 8098-8106.
10. Surroca Y, Haverkamp J, Heck AJR. Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of beta-lactoglobulin AB. J Chromatogr A. 2002; 970: 275-285.
11. Sugita Y, Okamoto Y. Replica-exchange molecular dynamics method for protein folding. Chem Phys Lett. 1999; 314: 141-151.
12. Euston SR. Molecular dynamics simulation of the effect of heat on the conformation of bovine beta-lactoglobulin A: a comparison of conventional and accelerated methods. Food Hydrocolloids. 2013; 30: 519-530.
13. Stənciuc N, Aprodu I, Râpeanu G, Bahrim G. Fluorescence spectroscopy and molecular modeling investigations on the thermally induced structural changes of bovine beta-lactoglobulin. Innov Food Sci Emerg Technol. 2012; 15: 50-56.
14. Seo JA, Hedoux A, Guinet Y, Paccou L, Affouard F, Lerbret A, Descamps M. Thermal denaturation of beta-lactoglobulin and stabilization mechanism by trehalose analyzed from raman spectroscopy investigations. J Phys Chem B. 2010; 114: 6675-6684.
15. Daura X, Mark AE, Gunsterenvan WF. Parametrization of aliphatic CHn united atoms of GROMOS96 force field. J Comput Chem. 1998; 19: 535-547.
16. Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, Simmerling C. Comparison of multiple amber force fields and development of improved protein backbone parameters. Proteins Struct Funct Bioinform. 2006; 65: 712-725.
17. Hess B, Kutzner C, Spoelvan der D, Lindahl E. GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput. 2008; 4: 435-447.
18. Sorin EJ, Pande VS. Exploring the helix-coil transition via all-atom equilibrium ensemble simulations. Biophys J. 2005; 88: 2472-2493.
19. Hess B, Bekker H, Berendsen HJC, Fraaije JGEM. LINCS: a linear constraint solver for molecular simulations. J Comput Chem. 1997; 18: 1463-1472.
20. Miyamoto S, Kollman PA. Settle: an analytical version of the shake and rattle algorithm for rigid water models. J Comput Chem. 1992; 13: 952-962.
21. Darden T, York D, Pedersen L. Particle mesh Ewald: an N ·log(n) method for Ewald sums in large systems. J Chem Phys. 1993; 98: 10089-10092.
22. Essmann U, Perera L, Berkowitz ML, Darden T, Lee H, Pedersen LG. A smooth particle mesh Ewald method. J Chem Phys. 1995; 103: 8577-8593.
23. Bussi G, Donadio D, Parrinello M. Canonical sampling through velocity rescaling. J Chem Phys. 2007; 126: 014101.
24. Parrinello M, Rahman A. Polymorphic transitions in single-crystals: a new molecular-dynamics method. J Appl Phys. 1981; 52: 7182-7190.
25. Coluzza I, Frenkel D. Virtual-move parallel tempering. Chemphyschem. 2005; 6: 1779-1783.
26. Periole X, Mark AE. Convergence and sampling efficiency in replica exchange simulations of peptide folding in explicit solvent. J Chem Phys. 2007; 126: 014903.
27. Marino KA, Bolhuis PG. Confinement-induced states in the folding landscape of the Trp-cage miniprotein. J Phys Chem B. 2012; 116: 11872-11880.
28. Creamer LK, Bienvenue A, Nilsson H, Paulsson M, Wanroijvan M, Lowe EK, Anema SG, Boland MJ, Flores Jimenez R. Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine beta-lactoglobulin. J Agric Food Chem. 2004; 52: 7660-7668.
29. Eberini I, Sensi C, Barbiroli A, Bonomi F, Iametti S, Galliano M, Gianazza E. Electrostatics of folded and unfolded bovine beta-lactoglobulin. Amino Acids. 2012; 42: 2019-2030.
30. Zeiler RNW, Bolhuis PG. Numerical study of the effect of thiol-disulfide exchange in the cluster phase of beta-lactoglobulin aggregation. Faraday Discuss. 2012; 158: 461-477.