Literature DB >> 2748579

Second virial coefficient of alpha-crystallin.

X W Wang1, F A Bettelheim.   

Abstract

Light scattering studies were performed on bovine alpha-crystallin measuring the scattering intensities as a function of scattering angle, concentration, and temperature. The data yielded the molecular weight, radius of gyration, and second virial coefficient of alpha-crystallin at different temperatures. The second virial coefficient increased with increasing temperature. Both the enthalpy and entropy of solution of alpha-crystallin are positive. The Flory theta temperature was found to be 271 K.

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Year:  1989        PMID： 2748579     DOI： 10.1002/prot.340050211

Source DB:  PubMed          Journal:  Proteins        ISSN： 0887-3585


  5 in total

1.  Study of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamily.

Authors:  S Abgar; J Vanhoudt; T Aerts; J Clauwaert
Journal:  Biophys J       Date:  2001-04       Impact factor: 4.033

Review 2.  Protein interactions in the calf eye lens: interactions between beta-crystallins are repulsive whereas in gamma-crystallins they are attractive.

Authors:  A Tardieu; F Vérétout; B Krop; C Slingsby
Journal:  Eur Biophys J       Date:  1992       Impact factor: 1.733

3.  Electrostatic origin of in vitro aggregation of human γ-crystallin.

Authors:  Benjamin G Mohr; Cassidy M Dobson; Scott C Garman; Murugappan Muthukumar
Journal:  J Chem Phys       Date:  2013-09-28       Impact factor: 3.488

4.  Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine alpha-crystallin proteins.

Authors:  J Z Xia; Q Wang; S Tatarkova; T Aerts; J Clauwaert
Journal:  Biophys J       Date:  1996-11       Impact factor: 4.033

Review 5.  Mechanism of suppression of protein aggregation by α-crystallin.

Authors:  Kira A Markossian; Igor K Yudin; Boris I Kurganov
Journal:  Int J Mol Sci       Date:  2009-03-19       Impact factor: 6.208
  5 in total

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