A possible chaperone-like quaternary structure for alpha-crystallin

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Structural differences between bovine A(1) and A(2) β-casein alter micelle self-assembly and influence molecular chaperone activity.

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Darwinian transformation of a 'scarcely nutritious fluid' into milk.

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Investigation of gammaE-crystallin target protein binding to bovine lens alpha-crystallin by small-angle neutron scattering.

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Related Experiment Videos

A possible chaperone-like quaternary structure for alpha-crystallin

Related Concept Videos

Invited review: Modeling milk stability.

Structural differences between bovine A(1) and A(2) β-casein alter micelle self-assembly and influence molecular chaperone activity.

Potent natural egg-laying stimulant for cabbage butterflyPieris rapae.

Invited review: Caseins and the casein micelle: their biological functions, structures, and behavior in foods.

Darwinian transformation of a 'scarcely nutritious fluid' into milk.

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A possible chaperone-like quaternary structure for alpha-crystallin

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