Physical-chemical studies on bovine eye lens proteins

Andries, Christiane; Backhovens, Hubert; Clauwaert, J.; Block, Jan De; Voeght, Frank De; Dhont, Christine

doi:10.1016/0014-4835(82)90058-6

Cited by 35 publications

(10 citation statements)

References 43 publications

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“…( 3 ) presents the diffusion decays for the native and cross-linked αB-crystallins. The SDC values correspond quite well to the previous light scattering self-diffusion measurements of α-crystallin [22]. Note that the diffusion decays could be well approximated by a single SDC.…”

Section: Resultssupporting

confidence: 87%

Subunit Mobility and the Chaperone Activity of Recombinant aB-Crystallin

Krushelnitsky¹,

Mukhametshina²,

Gogolev³

et al. 2008

Open Biochem J

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Section: Resultssupporting

confidence: 87%

Subunit Mobility and the Chaperone Activity of Recombinant aB-Crystallin

Krushelnitsky¹,

Mukhametshina²,

Gogolev³

et al. 2008

Open Biochem J

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“…For a number of concentrated solutions, dilutions down to 1 mg/ml were made and photon correlation measurements and sedimentation analysis were performed. The results were the same as before (Andries et al, 1982) proving that the concentration step induces no irreversible changes. Initial Decay: Angular Dependence.…”

Section: Photon Correlation Spectroscopysupporting

confidence: 72%

“…For the calculation of the scattering vector K, the refractive index of H20 was used. Corrections for an increase of n with concentration are at most 2 or 3% as estimated from the refractive index increment (Andries et al, 1982). To reduce the diffusion coefficients to standard conditions, the viscosity of the solvent was used.…”

Section: Photon Correlation Spectroscopymentioning

confidence: 99%

Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations

Andries¹,

Clauwaert²

1985

Biophysical Journal

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The bovine eye lens protein, alpha L crystallin, has been studied with photon correlation spectroscopy and statical light scattering in the concentration range up to 200 g/l in different solvent conditions. At higher concentration (c greater than 70 g/l) the scattering behavior is quite complicated, which results in nonexponential correlation functions. Three methods have been used for the analysis of these correlation functions, namely, cumulant analysis, sum of two exponentials analysis, and exponential sampling method. These methods resulted in very similar results. The highly concentrated solutions contain two scattering entities: the single alpha L crystallin and a rather heterogeneous population of large clusters. The statical light-scattering experiments can be interpreted in the same way and gave consistent results for the dimensions of the large scattering units. The formation of these clusters, which are strong light scatterers, is superimposed on an increasing degree of correlation between the bulk of the alpha L-crystallins, resulting in a net decrease of light scattering as a function of concentration.

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“…Given that experimental crystallin samples prepared for measurement of dn/dc need to be constituted in a solvent that replicates fluid found in the eye lens, the greatest variability in dn/dc values from different studies comes from the wavelength used for measurement. Most experimental studies on dn/dc of crystallins have used proteins from the bovine lens13303132 and some have concentrated on α-crystallins3132 and/or γ-crystallins30. Where all three broad classes of crystallins have been measured, dn/dc was found to be highest for γ-crystallins13.…”

Section: Discussionmentioning

confidence: 99%

Primary sequence contribution to the optical function of the eye lens

Mahendiran

Elie

Nebel

et al. 2014

Sci Rep

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The crystallins have relatively high refractive increments compared to other proteins. The Greek key motif in βγ-crystallins was compared with that in other proteins, using predictive analysis from a protein database, to see whether this may be related to the refractive increment. Crystallins with Greek keys motifs have significantly higher refractive increments and more salt bridges than other proteins with Greek key domains. Specific amino acid substitutions: lysine and glutamic acid residues are replaced by arginine and aspartic acid, respectively as refractive increment increases. These trends are also seen in S-crystallins suggesting that the primary sequence of crystallins may be specifically enriched with amino acids with appropriate values of refractive increment to meet optical requirements. Comparison of crystallins from five species: two aquatic and three terrestrial shows that the lysine/arginine correlation with refractive increment occurs in all species investigated. This may be linked with formation and maintenance of salt bridges.

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Physical-chemical studies on bovine eye lens proteins

Cited by 35 publications

References 43 publications

Subunit Mobility and the Chaperone Activity of Recombinant aB-Crystallin

Subunit Mobility and the Chaperone Activity of Recombinant aB-Crystallin

Photon correlation spectroscopy and light scattering of eye lens proteins at high concentrations

Primary sequence contribution to the optical function of the eye lens

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