A natural and readily available crowding agent: NMR studies of proteins in hen egg white

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 5, 2011, Pages 1408-1415

  Martorell, Gabriel ^a   Adrover, Miquel ^a,b   Kelly, Geoff ^b   Temussi, Piero Andrea ^b,c   Pastore, Annalisa ^b  

^a UNIVERSITAT DE LES ILLES BALEARS   (Spain)

^b NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Aggregation; Confinement; Cytoplasm; Folding; Stability

Indexed keywords

EGG WHITE; GLOBULAR PROTEIN;

ARTICLE; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE; PARAMETER; PRIORITY JOURNAL; PROTEIN STABILITY; PROTEIN STRUCTURE;

ANIMALS; CHICKENS; EGG WHITE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STABILITY; PROTEINS; TEMPERATURE;

BACTERIA (MICROORGANISMS);

EID: 79954517065     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22967     Document Type: Article

References (37)

1. Rivas G, Ferrone F, Herzfeld J. Life in a crowded world. EMBO Rep 2004; 5: 23-27.
2. Minton AP, Wilf J. Effect of macromolecular crowding upon the structure and function of an enzyme: glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 1981; 20: 4821-4826.
3. Minton AP. Confinement as a determinant of macromolecular structure and reactivity. Biophys J 1992; 63: 1090-1100.
4. Luby-Phelps K. Cytoarchitecture and physical properties of cytoplasm: volume, viscosity, diffusion, intracellular surface area. Int Rev Cytol 2000; 192: 189-221.
5. Ogston AG. On the interaction of solute molecules with porous networks. J Phys Chem 1970; 74: 668-669.
6. Minton AP. The influence of macromolecular crowding and macromolecular confinement on biochemical reactions in physiological media. J Biol Chem 2001; 276: 10577-10580.
7. Miklos AC, Li C, Sharaf NG, Pielak GJ. Volume exclusion and soft interaction effects on protein stability under crowded conditions. Biochemistry 2010; 49: 6984-6991.
8. Reckel S, Loehr F, Doetsch V. In-cell NMR spectroscopy. Chembiochem 2005; 6: 1601-1606.
9. Selenko P, Wagner G. Looking into live cells with in-cell NMR spectroscopy. J Struct Biol 2007; 158: 244-253.
10. Wang Y, Li C, Pielak GJ. Effects of proteins on protein diffusion. J Am Chem Soc 2010; 132: 9392-9397.
11. Adinolfi S, Trifuoggi M, Politou AS, Martin S, Pastore A. A structural approach to understanding the iron-binding properties of phylogenetically different frataxins. Hum Mol Genet 2002; 11: 1865-1877.
12. Nair M, Adinolfi S, Pastore C, Kelly G, Temussi PA, Pastore A. Solution structure of the bacterial frataxin orthologue, CyaY: mapping the iron binding sites. Structure 2004; 12: 2037-2048.
13. Adinolfi A, Nair M, Politou A, Bayer E, Martin S, Temussi PA, Pastore A. The factors governing the thermal stability of frataxin orthologues: how to increase a protein stability. Biochemistry 2004; 43: 6511-6518.
14. Pastore A, Martin SR, Politou A, Kondapalli KC, Stemmler T, Temussi PA. Unbiased cold denaturation: low- and high-temperature unfolding of yeast frataxin under physiological conditions. J Am Chem Soc 2007; 129: 5374-5375.
15. He Y, Alam SL, Proteasa SV, Zhang Y, Lesuisse E, Dancis A, Stemmler TL. Yeast frataxin solution structure, iron binding, and ferrochelatase interaction. Biochemistry 2004; 43: 16254-16262.
16. Piotto M, Saudek, V, Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions J Biomol NMR 1992; 2: 661-666.
17. Bax A, Ikura M, Kay LE, Torchia DA, Tschudin R. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins. J Magn Reson 1990; 86: 304-318.
18. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 1995; 6: 277-293.
19. Goddard TD, Kneller DG. SPARKY 3, San Francisco: University of California 2008.
20. Silverstein RM, Webster FX, Kiemle D. Spectrometric identification of organic compounds, New York: John Wiley & Sons; 2005, 7th ed. ISBN 978-0-471-39362-7.
21. Pastore C, Francese M, Sica F, Temussi PA, Pastore A. Understanding the binding properties of an unusual metal binding protein: a study of bacterial frataxin. Eur J Biochem 2007; 274: 4199-4210.
22. Maciejewski MW, Liu D, Prasad R, Wilson SH, Mullen GP. Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase beta. Correlation with DNA binding and dRP lyase activity. J Mol Biol 2000; 296: 229-253.
23. Lee D, Hilty C, Wider G, Wuthrich K. Effective correlation times of proteins from NMR relaxation interference. J Magn Res 2006; 178: 72-76.
24. Bagchia B, Relation between orientational correlation time and the self-diffusion coefficient of tagged probes in viscous liquids: a density functional theory analysis. J Chem Phys 2001; 115: 2207-2211.
25. Robinson Lang E, Rha C. Apparent shear viscosity of native egg white. Int J Food Sci Technol 1982; 17: 595-606.
26. Adrover M, Esposito V, Martorell G, Pastore A, Temussi PA. Understanding cold denaturation: the case study of Yfh1. J Am Chem Soc 132: 16240-16246.
27. Privalov PL. Cold denaturation of proteins. Crit Rev Biochem Mol Biol 1990; 25: 281-305.
28. Bolis D, Politou AS, Kelly G, Pastore A, Temussi PA. Protein stability in nanocages: a novel approach for influencing protein stability by molecular confinement. J Mol Biol 2004; 336: 203-212.
29. Eggers DK, Valentine JS. Molecular confinement influences protein structure and enhances thermal protein stability. Protein Sci 2001; 10: 250-261.
30. Lan EH, Dave BC, Fukuto JM, Dunn B, Zink JI, Valentine JS. Synthesis of sol-gel encapsulated heme proteins with chemical sensing properties. J Mater Chem 1999; 9: 45-53.
31. Gottfried DS, Kagan A, Hoffman BM, Friedman JM. Impeded rotation of a protein in a sol-gel matrix. J Phys Chem B 1999; 103: 2803-2807.
32. Zhou Y, Hall CK. Solute excluded-volume effects on the stability of globular proteins: a statistical thermodynamic theory. Biopolymers 1996; 38: 273-284.
33. Minton AP. Effect of a concentrated "inert" macromolecular cosolute on the stability of a globular protein with respect to denaturation by heat and by chaotropes: a statistical-thermodynamic model. Biophys J 2000; 78: 101-109.
34. Zhou HX. Protein folding in confined and crowded environments. Arch Biochem Biophys 2008; 469: 76-82.
35. Zhou HX. Protein folding and binding in confined spaces and in crowded solutions. J Mol Recognit 2004; 17: 368-375.
36. Ravindra R, Zhao S, Gies H, Winter R. Protein encapsulation in mesoporous silicate: the effects of confinement on protein stability, hydration, and volumetric properties. J Am Chem Soc 2004; 126: 12224-12225.
37. Peterson RW, Anbalagan K, Tommos C, Wand AJ. Forced folding and structural analysis of metastable proteins. J Am Chem Soc 2004; 126: 9498-9499.