Conformational variability of goat β-lactoglobulin: Crystallographic and thermodynamic studies

International Journal of Biological Macromolecules

Volumn 72, Issue , 2015, Pages 1283-1291

  Loch, Joanna I ^a   Bonarek, Piotr ^a   Polit, Agnieszka ^a   Światek, Sylwia ^a,b   Czub, Mateusz ^a   Ludwikowska, Mira ^a   Lewiński, Krzysztof ^a  

^a JAGIELLONIAN UNIVERSITY   (Poland)

^b INSTITUTE OF CATALYSIS AND SURFACE CHEMISTRY   (Poland)

Author keywords

Asymmetric dimer; Goat milk; lactoglobulin

Indexed keywords

BETA LACTOGLOBULIN; DODECYL SULFATE SODIUM; LIPOCALIN; LACTOGLOBULIN; PROTEIN BINDING;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL; CRYSTALLOGRAPHY; DIMERIZATION; ENERGY; ENTHALPY; ENTROPY; GOAT MILK; LIGAND BINDING; PH; PROTEIN BINDING; PROTEIN CONFORMATION; THERMODYNAMICS; ANIMAL; BOVINE; CALORIMETRY; CHEMISTRY; CIRCULAR DICHROISM; GOAT; METABOLISM; PROTEIN MULTIMERIZATION; PROTEIN SECONDARY STRUCTURE; SPECTROFLUOROMETRY; TIME; ULTRAVIOLET SPECTROPHOTOMETRY; X RAY CRYSTALLOGRAPHY;

BOVINAE; CAPRA HIRCUS;

ANIMALS; CALORIMETRY; CATTLE; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; GOATS; LACTOGLOBULINS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; SODIUM DODECYL SULFATE; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; THERMODYNAMICS; TIME FACTORS;

EID: 84918546312     PISSN: 01418130     EISSN: 18790003     Source Type: Journal    
DOI: 10.1016/j.ijbiomac.2014.10.031     Document Type: Article

References (52)

1. Sawyer L. Advanced Dairy Chemistry, Volume 1A: Proteins: Basic Aspects 2013, 211-259. Springer, New York. 4th Edition.
2. Kontopidis G., Holt C., Sawyer L. Dairy Sci. 2004, 87:785-796.
3. Pérez M.D., Sanchez L., Aranda P., Ena J.M., Oria R., Calvo M. BBA-Lipid Lipid Met. 1992, 1123:151-155.
4. Kontopidis G., Holt C., Sawyer L. Mol. Biol. 2002, 318:1043-1055.
5. Palmer A.H. J. Biol. Chem. 1934, 104:359-372.
6. Pérez M.D., Díaz de Villegas C., Sánchez L., Aranda P., Ena J.M., Calvo M. J. Biochem. 1989, 106:1094-1097.
7. Kumar A., Rout P.K., Roy R.J. Appl. Genet. 2006, 47:49-53.
8. Folch J.M., Coll A., Sanchez A.J. Dairy Sci. 1994, 77:3493-3497.
9. Bain J.A., Deutsch H.F. Arch. Biochem. Biophys. 1948, 16:221-229.
10. Askonas B.A. Biochem. J. 1954, 58:332-336.
11. Townend R., Kumosinski T.F., Timasheff S.N. J. Biol. Chem. 1967, 242:4538-4545.
12. Pace C.N., Alexander S.S. Biochemistry 1971, 10:2738-2743.
13. Townend R., Basch J.J. Arch. Biochem. Biophys. 1968, 126:59-66.
14. Sawyer L., Kontopidis G. Biochim. Biophys. Acta 2000, 1482:136-148.
15. Burova T.V., Rabesona H., Choiset Y., Jankowski C.K., Sawyer L., Haertlé T. Biochim. Biophys. Acta 2000, 1478:267-279.
16. Åkerstrom B., Flower D.R., Salier J.P. Biochim. Biophys. Acta 2000, 1482:1-8.
17. Tanford C., Bunville L.G., Nozaki Y.T. J. Am. Chem. Soc. 1959, 81:4032-4036.
18. Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., Jameson G.B. Biochemistry 1998, 37:14014-14023.
19. Skerra A. FEBS J. 2008, 275:2677-2683.
20. Mross K., Richly H., Fischer R., Scharr D., Büchert M., Stern A., Gille H., Audoly L.P., Scheulen M.E. PLoS One 2013, 8:e83232.
21. Loch J.I., Bonarek P., Polit A., Światek S., Dziedzicka-Wasylewska M., Lewiński K. J. Mol. Recognit. 2013, 8:357-367.
22. Blanc F., Bernard H., Alessandri S., Bublin M., Paty E., Leung S.A., Patient K.A., Wal J.M. Mol. Nutr. Food Res. 2008, 52:S166-S175.
23. Neyestani T.R., Djalali M., Pezeshki M. Protein Expr. Purif. 2003, 29:202-208.
24. Dufour E., Marden M.C., Haertlé T. FEBS Lett. 1990, 277:223-226.
25. Evans P.R. Acta Cryst. 2011, D67:282-292.
26. Winn M.D., Ballard C.C., Cowtan K.D., Dodson E.J., Emsley P., Evans P.R., Keegan R.M., Krissinel E.B., Leslie A.G., McCoy A., McNicholas S.J., Murshudov G.N., Pannu N.S., Potterton E.A., Powell H.R., Read R.J., Vagin A., Wilson K.S. Acta Cryst. 2011, D67:235-242.
27. Kabsch W. Acta Cryst. 2010, D66:125-132.
28. McCoy A.J., Grosse-Kunstleve R.W., Adams P.D., Winn M.D., Storoni L.C., Read R.J. J. Appl. Crystallogr. 2007, 40:658-674.
29. Murshudov G.N., Skubák P., Lebedev A.A., Pannu N.S., Steiner R.A., Nicholls R.A., Winn M.D., Long F., Vagin A.A. Acta Cryst. 2011, D67:355-367.
30. Emsley P., Lohkamp B., Scott W.G., Cowtan K. Acta Cryst. 2010, D66:486-501.
31. Strickland E.H. CRC Crit. Rev. Biochem. 1974, 2:113-175.
32. Manderson G.A., Hardman M.J., Creamer L.K. J. Agric. Food Chem. 1999, 47:3617-4327.
33. Bello M., Pérez-Hernández G., Fernández-Velasco D.A., Arreguín-Espinosa R., García-Hernández E. Proteins 2008, 70:1475-1487.
34. Bello M., Portillo-Téllez Mdel C., García-Hernández E. Biochemistry 2011, 50:151-161.
35. Renard D., Lefebvre J., Griffin M.C.A., Griffin W.G. Int. J. Biol. Macromol. 1998, 22:41-49.
36. Vijayalakshmi L., Krishna R., Sankaranarayanan R., Vijayan M. Proteins 2008, 71:241-249.
37. Oliveira K.M.G., Valente-Mesquita V.L., Botelho M.M., Sawyer L., Ferreira S.T., Polikarpov I. Eur. J. Biochem. 2001, 268:477-483.
38. Qin B.Y., Bewley M.C., Creamer L.K., Baker E.N. Protein Sci. 1999, 8:75-83.
39. Sawyer L., Kontopidis G., Wu S.-Y. Int. J. Food Sci. Technol. 1999, 34:409-418.
40. Adams J.J., Anderson B.F., Norris G.E., Creamer L.K., Jameson G.B. J. Struct. Biol. 2006, 154:246-254.
41. Brownlow S., Morais Cabral J.H., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C., Sawyer L. Structure 1997, 5:481-495.
42. Sakurai K., Goto Y.J. Mol. Biol. 2006, 356:483-496.
43. Creamer L.K. Biochemistry 1995, 34:7170-7176.
44. Waninge R., Paulsson M., Nylander T., Ninham B., Sellers P. Int. Dairy J. 1998, 8:141-148.
45. Considine T., Patel H.A., Singh H., Creamer L.K. J. Agric. Food Chem. 2005, 53:3197-3205.
46. Hu W., Liu J., Luo Q., Han Y., Wu K., Lv S., Xiong S., Wang F. Rapid Commun. Mass Spectrom. 2011, 25:1429-1436.
47. Jones M.N., Wilkinson A. Biochem. J. 1976, 153:713-718.
48. Kresheck G.C., Hargraves W.A., Mann D.C. J. Phys. Chem. 1977, 81:532-537.
49. Jung J.M., Savin G., Pouzot M., Schmitt C., Mezzenga R. Biomacromolecules 2008, 9:2477-2486.
50. Loch J.I., Bonarek P., Polit A., Riès D., Dziedzicka-Wasylewska M., Lewiński K. Int. J. Biol. Macromol. 2013, 57:226-231.
51. Loch J.I., Polit A., Bonarek P., Olszewska D., Kurpiewska K., Dziedzicka-Wasylewska M., Lewiński K. Int. J. Biol. Macromol. 2012, 50:1095-1102.
52. Gutiérrez-Magdaleno G., Bello M., Portillo-Téllez M.C., Rodríguez-Romero A., García-Hernández E.J. Mol. Recognit. 2013, 26:67-75.