Mutant bovine odorant-binding protein: Temperature affects the protein stability and dynamics as revealed by infrared spectroscopy and molecular dynamics simulations

Proteins: Structure, Function and Genetics

Volumn 72, Issue 2, 2008, Pages 769-778

  Marabotti, Anna ^a   Lefèvre, Thierry ^b   Staiano, Maria ^c   Crescenzo, Roberta ^c   Varriale, Antonio ^c   Rossi, Mosè ^c   Pézolet, Michel ^b   D'Auria, Sabato ^c  

^a CNR   (Italy)

^b UNIVERSITÉ LAVAL   (Canada)

^c INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

FTIR spectroscopy; Odorant binding protein; Protein conformation; Protein dynamics

Indexed keywords

DISULFIDE; MUTANT PROTEIN; ODORANT BINDING PROTEIN; PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; COW; INFRARED SPECTROSCOPY; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STABILITY; SIMULATION;

ANIMALS; CATTLE; MUTATION; RECEPTORS, ODORANT; SPECTROPHOTOMETRY, INFRARED;

BOVINAE;

EID: 46449107710     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21966     Document Type: Article

References (32)

1. Bignetti E, Cavaggioni A, Pelosi P, Persaud KC, Sorbi RT, Tirindelli R. Purification and characterisation of an odorant-binding protein from cow nasal tissue. Eur J Biochem 1985;149:227-231.
2. Bianchet MA, Bains G, Pelosi P, Pevsner J, Snyder SH, Monaco HL, Amzel LM. The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition. Nat Struct Biol 1996;3:934-939.
3. Tegoni M, Ramoni R, Bignetti E, Spinelli S, Cambillau C. Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nat Struct Biol 1996;3:863-867.
4. Flower DR, North AC, Sansom CE. The lipocalin protein family: structural and sequence overview. Biochim Biophys Acta 2000;1482:9-24.
5. Grzyb J, Latowski D, Strzalka K. Lipocalins - a family portrait. J Plant Physiol 2006;163:895-915.
6. Tegoni M, Pelosi P, Vincent F, Spinelli S, Campanacci V, Grolli S, Ramoni R, Cambillau C. Mammalian odorant binding proteins. Biochim Biophys Acta 2000;1482:229-240.
7. Ramoni R, Vincent F, Ashcroft AE, Accornero P, Grolli S, Valencia C, Tegoni M, Cambillau C. Control of domain swapping in bovine odorant-binding protein. Biochem J 2002;365:739-748.
8. Spinelli S, Ramoni R, Grolli S, Bonicel J, Cambillau C, Tegoni M. The structure of the monomeric porcine odorant binding protein sheds light on the domain swapping mechanism. Biochemistry 1998;37:7913-7918.
9. Vincent F, Spinelli S, Ramoni R, Grolli S, Pelosi P, Cambillau C, Tegoni M. Complexes of porcine odorant binding protein with odorant molecules belonging to different chemical classes. J Mol Biol 2000;300:127-139.
10. Casal HL, Köhler U, Mantsch HH. Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature Biochim Biophys Acta 1988;957:11-20.
11. Paolini S, Tanfani F, Fini C, Bertoli E, Pelosi P. Porcine odorant-binding protein: structural stability and ligand affinities measured by Fourier-transform infrared spectroscopy and fluorescence spectroscopy. Biochim Biophys Acta 1999;1431:179-188.
12. Lefevre T, Subirade M. Molecular differences in the formation and structure of fine-stranded and particulate β-lactoglobulin gels. Biopolymers 2000;54:578-586.
13. Marabotti A, Ausili A, Staiano M, Scirè A, Tanfani F, Parracino A, Varriale A, Rossi M, D'Auria S. Pressure affects the structure and the dynamics of the D-galactose/D-glucose-binding protein from Escherichia coli by perturbing the C-terminal domain of the protein. Biochemistry 2006;45:11885-11894.
14. Stepanenko OV, Marabotti A, Kuznetsova IM, Turoverov KK, Fini C, Varriale A, Staiano M, Rossi M, D'Auria S. Hydrophobic interactions and ionic networks play an important role in thermal stability and denaturation mechanism of the porcine odorant-binding protein. Proteins; Published online ahead of print, DOI: 10.1002/prot.21658.
15. Berman H, Henrick K, Nakamura H, Markley JL. The worldwide Protein Data Bank (wwPDB): ensuring a single, uniform archive of PDB data. Nucleic Acids Res 2007;35(Database Issue):D301-D303.
16. Lindahl E, Hess B, van der Spoel D. GROMACS 3.0: a package for molecular simulation and trajectory analysis. J Mol Model 2001;7:306-317.
17. van der Spoel D, Lindahl E, Hess B, Groenhof G, Mark AE, Berendsen HJ. GROMACS: fast, flexible and free. J Comput Chem 2005;26:1701-1718.
18. van Gunsteren WF, Billeter SR, Eising AA, Hunenberger PH, Kruger P, Mark AE, Scott WRP, Tironi IG. Biomolecular simulation: The GROMOS96 manual and user guide. Zurich, Switzerland: Vdf Hochschulverlag AG an der ETH Zurich; 1996. 1042 p.
19. Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J. Interaction models for water in relation to protein hydration. In: Pullman B, editor. Intermolecular forces. Dordrecht: Reidel D. Publishing Company; 1981, pp 331-342.
20. Hess B, Bekker H, Berendsen HJC, Fraaije JGEM. LINCS: a linear constraint solver for molecular simulations. J Comput Chem 1997;18:1463-1472.
21. Berendsen HJC, Postma JPM, Di Nola A, Haak JR. MD with coupling to an external bath. J Phys Chem 1984;81:3684-3690.
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. Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers 1983;22:2577-2637.
24. Hubbard SJ, Campbell SF, Thornton JM. Molecular recognition. Conformational analysis of limited proteolytic sites and serine proteinase protein inhibitors. J Mol Biol 1991;220:507-530.
25. Kumar S, Nussinov R. Salt bridge stability in monomeric proteins. J Mol Biol 1999;293:1241-1255.
26. Krimm S, Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv Protein Chem 1986;38:181-364.
27. 2O) solutions. I. Spectral parameters of amino acid residue absorption bands. Biopolymers 1990;30: 1243-1257.
28. Timasheff SN, Susi H, Stevens L. Infrared spectra and protein conformations in aqueous solution. II. Survey of globular proteins. J Biol Chem 1967;242:5467-5473.
29. Clark AH, Saunderson DH, Suggett A. Infrared and laser-Raman spectroscopic studies of thermally-induced globular protein gels. Int J Pept Protein Res 1981;17:353-364.
30. Papiz MZ, Sawyer L, Eliopoulos EE, North AC, Findlay JB, Sivaprasadarao R, Jones TA, Newcomer ME, Kraulis PJ. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 1986;324:383-385.
31. Ferry JD. Protein gels. Adv Protein Chem 1948;4:1-78.
32. Ramoni R, Bellucci S, Grycznyski I, Grycznyski Z, Grolli S, Staiano M, Giannini G, Micciulla F, Pastore R, Tiberia A, Conti V, Merli E, Varriale A, Rossi M, D'Auria S. The protein scaffold of the lipocalin odorant binding protein is suitable for the development of biosensors for the detection of explosive components. J Opt Phys Solid Matter 2007;19:395012-395019.