PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2012 | 59 | 2 |

Tytuł artykułu

Denaturation and aggregation of lysozyme in water-ethanol solution

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
We have applied rheological methods for the analysis of ethanol-lysozyme interaction during the process of denaturation and aggregation of the protein. At low concentration of ethanol a destruction of the hydration shell of lysozyme is observed. With the increase in the ethanol concentration a structural transformation takes place. It leads to the formation of a protein aggregate with an elongated structure. The rheological characteristics of lysozyme-water-ethanol solution changes from Newtonian to pseudoplastic.

Słowa kluczowe

Wydawca

-

Rocznik

Tom

59

Numer

2

Opis fizyczny

p.317-321,fig.,ref.

Twórcy

autor
  • Faculty of Physics, Department of Molecular Biophysics, Adam Mickiewicz University, Poznan, Poland
autor
autor

Bibliografia

  • Ahmad F, Salahuddin A (1974) Influence of temperature on the intrinsic viscosities of proteins in random coil conformations. Biochemistry 13: 245-249. 
  • Akasaka K, Latif AR, Nakamura A, Matsuo K, Tachibana H, Gekko K (2007) Amyloid protofibril is highly voluminous and compressible. Biochemistry 46: 10444-10450. 
  • Areas EPG, Areas JAG, Hamburger J, Peticolas WL, Santos PS (1996) On the high viscosity of aqueous solution of lysozyme induced by some organic solvents. J Coll Inter Sci 180: 578-589.
  • Bhattacharjya S, Balaram P (1997) Effects of organic solvents on protein structures: observation of a structured helical core in hen egg white lysozyme in aqueous dimethylsulfoxide. Proteins 29: 492-507. 
  • Cao A, Hu D, Lai L (2004) Formation of amyloid fibrils from fully reduced hen egg white lysozyme. Protein Sci 13: 319-324. 
  • Chalikian TV, Filfil R (2003) How large are the volume changes accompanying protein transitions and binding? Biophys Chem 104: 489-499. 
  • Deshpande A, Nimsadkar S, Mande SC (2005) Effect of alcohols on protein hydration: crystallographic analysis of hen egg-white lysozyme in the presence of alcohols. Acta Crystallogr D Biol Crystallogr 61: 1005-1008. 
  • Frare E, Polverino de Laureto P, Zurdo J, Dobson ChM, Fontana A (2004) A highly amyloidogenic region of hen lysozyme. J Mol Biol 340: 1153-1165. 
  • Fujiwara S, Matsumoto F, Yonezawa Y (2003) Effects of salt concentration on association of the amyloid protofilaments of hen egg white lysozyme studied by time-resolved neutron scattering. J Mol Biol 331: 21-28. 
  • Gekko K, Hasegawa Y (1986) Compressibility - structure relationship of globular proteins. Biochemistry 25: 6563-6571. 
  • Goda S, Takano K, Yamagata Y, Nagata R, Akutsu H, Maki S, Namba K, Yutani K (2000) Amyloid protofilament formation of hen egg lysozyme in highly concentrated ethanol solution. Protein Sci 9: 369-375. 
  • Harding SE (1997) The intrinsic viscosity of biological macromolecules. Progress in measurement, interpretation and application to structure in dilute solution. Prog Biophys Mol Biol 68: 207-262. 
  • Holley M, Eginton Ch, Schaefer D, Brown LR (2008) Characterization of amyloidogenesis of hen egg lysozyme in concentrated ethanol solution. Biochem Biophys Res Commun 373: 164-168. 
  • Kamiyama T, Matsusita T, Kimura T (2003) Volumetric study of lysozyme in dimethyl sulfoxide+water solution at 298.15 K. J Chem Eng Data 48: 1301-1305.
  • Kamiyama T, Morita M, Kimura T (2004) Rheological study of lysozyme in dimethyl sulfoxide+water solution at 298.15 K. J Chem Eng Data 49: 1350-1353.
  • Krebs HRM, Wilkins KD, Chung WE, Pitkeathly CM, Chamberlain KA, Zurdo J, Robinson VC, Dobson ChM (2000) Formation and seeding of amyloid fibrils from wild- type hen lysozyme and a peptide fragment from the b-domain. J Mol Biol 300: 541-549. 
  • Lefebvre J (1982) Viscosity of concentrated protein solutions. Rheol Acta 21: 620-625.
  • Lehmann MS, Mason SA, McIntyre GJ (1985) Study of ethanol-lysozyme interaction using neutron diffraction. Biochemistry 24: 5862-5869. 
  • Matagne A, Jamin M, Chung EW, Robinson CV, Radford SE, Dobson ChM (2000) Thermal unfolding of an intermediate is associated with non-arrhenius kinetics in the folding of hen lysozyme. J Mol Biol 297: 193-210. 
  • Matagne A, Radford SE, Dobson ChM (1997) Fast and slow tracks in lysozyme folding: insight into the role of domains in the folding process. J Mol Biol 267: 1068-1074. 
  • Monkos K. (1997) Concentration and temperature dependence of viscosity in lysozyme aqueous solutions. Biochim Biophys Acta 1339: 304-310. 
  • Pan W, Filobelo L, Pham NDQ, Galkin O, Uzunova VV, Vekilov PG (2009) Viscoelasticity in homogeneous protein solutions. Phys Rev Lett 102: 058101-1-058101-4. 
  • Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennet GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, Feest TG, Zalin AM, Hsuan JJ (1993) Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature 362: 553-557. 
  • Sasahara K, Sakurai M, Nitta K (1999) The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding. J Mol Biol 291: 693-701. 
  • Schweiker KL, Fitz VW, Makhatadze GI (2009) Universal convergence of the specific volume changes of globular proteins upon unfolding. Biochemistry 48: 10846-10851. 
  • Sirotkin VA, Winter R (2010) Volume changes associate with guanidine hydrochloride, temperature and ethanol induced unfolding of lysozyme. J Phys Chem 114: 16881-16886. 
  • Stefani M, Dobson ChM (2003) Protein aggregation and aggregate toxicity; new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 81: 678-699. 
  • Szymańska A, Ślósarek G (2012) Light scattering studies of hydration and structural transformations of lysozyme. Acta Phys Pol A 121: 694-698.
  • Tanford C, Kawahara K, Lapanje S (1967) Proteins as random coils. I. intrinsic viscosities and sedimentation coefficients in concentrated guanidine hydrochloride. J Am Chem Soc 89: 5023-5029. 
  • Trexler AJ, Nilsson MR (2007) The formation of amyloid fibrils from proteins in the lysozyme family. Curr Protein Pept Sci 8: 537-557. 
  • Uversky VN, Fink AL (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded, Biochim Biophys Acta 1698: 131-153. 
  • Yonezawa Y, Tanaka S, Kubota T, Wakabayashi K, Yutani K, Fujiwara S (2002) An insight into the pathway of the amyloid fibril formation of hen egg white lysozyme obtained from a small-angle x-ray and neutron scattering study. J Mol Biol 323: 237-251. 
  • Zhou H (1995) Calculation of translational friction and intrinsic viscosity. II. Application to globular proteins. Biophys J 69: 2298-2303. 

Uwagi

PL
Rekord w opracowaniu.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-c0799a48-1eab-43ef-8411-f255cdcf3293
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.