Electrostatics of folded and unfolded bovine β-lactoglobulin

Amino Acids

Volumn 42, Issue 5, 2012, Pages 2019-2030

  Eberini, Ivano ^a   Sensi, Cristina ^a   Barbiroli, Alberto ^a   Bonomi, Franco ^a   Iametti, Stefania ^a   Galliano, Monica ^b   Gianazza, Elisabetta ^a  

^a UNIVERSITY OF MILAN   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

Author keywords

Bovine lactoglobulin; Electrophoresis; Electrostatics; Molecular modeling; Unfolding; Urea

Indexed keywords

AMINO ACID; BETA LACTOGLOBULIN; GLUTAMIC ACID; HISTIDINE; UREA;

AMINO ACID ANALYSIS; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONCENTRATION RESPONSE; COW; CRYSTAL STRUCTURE; DENATURING GRADIENT GEL ELECTROPHORESIS; FLUORESCENCE SPECTROSCOPY; HYDROGEN BOND; ISOELECTRIC FOCUSING; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; STATIC ELECTRICITY; STRUCTURE ANALYSIS; TITRIMETRY;

AMINO ACIDS; ANIMALS; CATTLE; CIRCULAR DICHROISM; ELECTROPHORESIS; HYDROGEN-ION CONCENTRATION; KINETICS; LACTOGLOBULINS; MOLECULAR DYNAMICS SIMULATION; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN ISOFORMS; PROTEIN UNFOLDING; SOLVENTS; STRUCTURE-ACTIVITY RELATIONSHIP;

BOVINAE;

EID: 84862759734     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-011-0933-z     Document Type: Article

References (51)

1. Aguilar B, Anandakrishnan R, Ruscio JZ, Onufriev AV (2010) Statistics and physical origins of pK and ionization state changes upon protein-ligand binding. Biophys J 98:872-880
2. Barbiroli A, Beringhelli T, Bonomi F, Donghi D, Ferranti P, Galliano M, Iametti S, Maggioni D, Rasmussen P, Scanu S, Vilardo MC (2010) Bovine beta-lactoglobulin acts as an acid-resistant drug carrier by exploiting its diverse binding regions. Biol Chem 391:21-32
3. Beringhelli T, Eberini I, Galliano M, Pedoto A, Perduca M, Sportiello A, Fontana E, Monaco HL, Gianazza E (2002) pH and ionic strength dependence of protein (un)folding and ligand binding to bovine b-lactoglobulins A and B. Biochemistry 41:15415-15422 (Pubitemid 36008153)
4. Bjellqvist B, Ek K, Righetti PG, Gianazza E, Görg A, Postel W, Westermeier R (1982) Isoelectric focusing in immobilized pH gradients: principles, methodology and some applications. J Biochem Biophys Methods 6:317-339
5. Creighton TE (1979) Electrophoretic analysis of the unfolding of proteins by urea. J Mol Biol 129:235-264
6. Creighton TE (1980) Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J Mol Biol 137:61-80
7. D'Alfonso L, Collini M, Baldini G (2002) Does b-lactoglobulin denaturation occur via an intermediate state? Biochemistry 41:326-333 (Pubitemid 34051328)
8. Eberini I, Baptista AM, Gianazza E, Fraternali F, Beringhelli T (2004) Reorganization in apo- and holo-b-lactoglobulin upon protonation of Glu89: molecular dynamics and pKa calculations. Proteins 54:744-758 (Pubitemid 38298793)
9. Ellis RJ, van der Vies SM (1991) Molecular chaperones. Annu Rev Biochem 60:321-347
10. Fessas D, Iametti S, Schiraldi A, Bonomi F (2001) Thermal unfolding of monomeric and dimeric beta-lactoglobulins. Eur J Biochem 268:5439-5448 (Pubitemid 32948371)
11. Fogolari F, Ragona L, Licciardi S, Romagnoli S, Michelutti R, Ugolini F, Molinari H (2000) Electrostatic properties of bovine b-lactoglobulin. Proteins 39:317-330
12. Gianazza E, Giacon P, Sahlin B, Righetti PG (1985) Non-linear pH courses with immobilized pH gradients. Electrophoresis 6:53-56
13. Gianazza E, Galliano M, Miller I (1997) Structural transitions of human serum albumin: an investigation using electrophoretic techniques. Electrophoresis 18:695-700 (Pubitemid 27226967)
14. Gianazza E, Castiglioni S, Eberini I (1999) Low-tech electrophoresis, small but beautiful, and effective: electrophoretic titration curves of proteins. Electrophoresis 20:1325-1338 (Pubitemid 29299979)
15. Gitlin I, Carbeck JD, Whitesides GM (2006) Why are proteins charged? Networks of charge-charge interactions in proteins measured by charge ladders and capillary electrophoresis. Angew Chem Int Ed Engl 45:3022-3060 (Pubitemid 44099016)
16. Gohda K, Hakoshima T (2008) A molecular mechanism of P-loop pliability of Rho-kinase investigated by molecular dynamic simulation. J Comput Aided Mol Des 22:789-797
17. Goldberg AL (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 426:895-899 (Pubitemid 38056882)
18. Goldenberg DP (1989) Analysis of protein conformation by gel electrophoresis. In: Creighton TE (ed) Protein structure: a practical approach. IRL Press, Oxford, pp 225-250
19. Goldenberg NM, Steinberg BE (2010) Surface charge: a key determinant of protein localization and function. Cancer Res 70:1277-1280
20. Harris TK, Turner GJ (2002) Structural basis of perturbed pKa values of catalytic groups in enzyme active sites. IUBMB Life 53:85-98 (Pubitemid 34553129)
21. Iametti S, De Gregori B, Vecchio G, Bonomi F (1996) Modifications occur at different structural levels during the heat denaturation of beta-lactoglobulin. Eur J Biochem 237:106-112 (Pubitemid 26110279)
22. Iametti S, Scaglioni L, Mazzini S, Vecchio G, Bonomi F (1998) Structural features and reversible association of different quaternary structures of b-lactoglobulin. J Agric Food Chem 46:2159-2166 (Pubitemid 128491127)
23. Iametti S, Rasmussen P, Frokiaer H, Ferranti P, Addeo F, Bonomi F (2002) Proteolysis of bovine beta-lactoglobulin during thermal treatment in subdenaturing conditions highlights some structural features of the temperature-modified protein and yields fragments with low immunoreactivity. Eur J Biochem 269:1362-1372 (Pubitemid 34228909)
24. Juffer AH (1998) Theoretical calculations of acid-dissociation constants of proteins. Biochem Cell Biol 76:198-209 (Pubitemid 29102005)
25. Kolossváry I, Keserü GM (2001) Hessian-free low-mode conformational search for large-scale protein loop optimization: application to c-jun N-terminal kinase JNK3. J Comput Chem 22:21
26. Labute P (2010) LowModeMD-implicit low-mode velocity filtering applied to conformational search of macrocycles and protein loops. J Chem Inf Model 50:792-800
27. Lanni C, Uberti D, Racchi M, Govoni S, Memo M (2007) Unfolded p53: a potential biomarker for Alzheimer's disease. J Alzheimers Dis 12:93-99 (Pubitemid 47396308)
28. Lee AC, Crippen GM (2009) Predicting pKa. J Chem Inf Model 49:2013-2033
29. Li H, Robertson AD, Jensen JH, Vacca JP (2005) Very fast empirical prediction and rationalization of protein pKa values. Proteins 61:704-721 (Pubitemid 41753142)
30. Lozinsky E, Iametti S, Barbiroli A, Likhtenshtein GI, Kalai T, Hideg K, Bonomi F (2006) Structural features of transiently modified beta-lactoglobulin relevant to the stable binding of large hydrophobic molecules. Protein J 25:1-15 (Pubitemid 43806845)
31. Monaco HL, Zanotti G, Spadon P, Bolognesi M, Sawyer L, Eliopoulos EE (1987) Crystal structure of the trigonal form of bovine b-lactoglobulin and of its complex with retinol at 2.5 A ̊ resolution. J Mol Biol 197:695-706
32. Mulgrew-Nesbitt A, Diraviyam K, Wang J, Singh S, Murray P, Li Z, Rogers L, Mirkovic N, Murray D (2006) The role of electrostatics in protein-membrane interactions. Biochim Biophys Acta 1761:812-826 (Pubitemid 44332331)
33. Nakamura H (1996) Roles of electrostatic interaction in proteins. Q Rev Biophys 29:1-90 (Pubitemid 26190831)
34. Neves-Petersen MT, Petersen SB (2003) Protein electrostatics: a review of the equations and methods used to model electrostatic equations in biomolecules-applications in biotechnology. Biotechnol Annu Rev 9:315-395 (Pubitemid 41081513)
35. Nielsen JE, McCammon JA (2003) Calculating pKa values in enzyme active sites. Protein Sci 12:1894-1901 (Pubitemid 37022812)
36. Pace CN, Grimsley GR, Scholtz JM (2009) Protein ionizable groups: pK values and their contribution to protein stability and solubility. J Biol Chem 284:13285-13289
37. Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB (1998) Structural basis of the Tanford transition of bovine b-lactoglobulin. Biochemistry 37:14014-14023 (Pubitemid 28471234)
38. Rasmussen P, Barbiroli A, Bonomi F, Faoro F, Ferranti P, Iriti M, Picariello G, Iametti S (2007) Formation of structured polymers upon controlled denaturation of beta-lactoglobulin with different chaotropes. Biopolymers 86:57-72 (Pubitemid 46716695)
39. Righetti PG (1990) Immobilized pH gradients: theory and methodology. Elsevier, Amsterdam
40. Righetti PG, Drysdale JW (1974) Isoelectric focusing in gels. J Chromatogr 98:271-321
41. Righetti PG, Gianazza E (1980) pH-mobility curves of proteins by isoelectric focusing combined with electrophoresis at right angle. In: Radola BJ (ed) Electrophoresis '79. W. de Gruyter, Berlin, pp 23-38
42. Rochu D, Ducret G, Ribes F, Vanin S, Masson P (1999) Capillary zone electrophoresis with optimized temperature control for studying thermal denaturation of proteins at various pH. Electrophoresis 20:1586-1594 (Pubitemid 29300009)
43. Rosengren A ̊ , Bjellqvist B, Gasparic V (1977) A simple method of choosing optimum pH conditions for electrophoresis. In: Radola BJ, Graesslin D (eds) Electrofocusing and isotachophoresis. W. de Gruyter, Berlin, pp 165-171
44. Schreiber G, Shaul Y, Gottschalk KE (2006) Electrostatic design of protein-protein association rates. Methods Mol Biol 340:235-249
45. Shalabi SI, Fox PF (1982) Heat stability of milk: influence of cationic detergents on pH sensitivity. J Dairy Res 49:597-605
46. Sillero A, Maldonado A (2006) Isoelectric point determination of proteins and other macromolecules: oscillating method. Comput Biol Med 36:157-166 (Pubitemid 43028490)
47. Tanford C (1962) The interpretation of hydrogen titration curves of proteins. Adv Prot Chem 17:69-165
48. Tanford C, Bunville LG, Nozaki Y (1959) The reversible transformation of b-lactoglobulin at pH 7.5. J Am Chem Soc 81:4032-4036
49. Tyedmers J, Mogk A, Bukau B (2010) Cellular strategies for controlling protein aggregation. Nat Rev Mol Cell Biol 11:777-788
50. Vizcarra CL, Mayo SL (2005) Electrostatics in computational protein design. Curr Opin Chem Biol 9:622-626 (Pubitemid 41612190)
51. Wilson MR, Yerbury JJ, Poon S (2008) Potential roles of abundant extracellular chaperones in the control of amyloid formation and toxicity. Mol Biosyst 4:42-52 (Pubitemid 350261753)