Quaternary structure of bovine alpha-crystallin: influence of temperature. (Q47896985)

6 February 2018

title

Quaternary structure of bovine alpha-crystallin: influence of temperature. (English)

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6 February 2018

author name string

Vanhoudt J

1

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6 February 2018

Aerts T

2

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6 February 2018

Abgar S

3

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6 February 2018

Clauwaert J

4

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6 February 2018

publication date

1 May 1998

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6 February 2018

number of pages

9

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International Journal of Biological Macromolecules

inferred from page(s)

published in

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6 February 2018

volume

22

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6 February 2018

issue

3-4

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6 February 2018

page(s)

229-237

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6 February 2018

Theory of transparency of the eye.

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Short-range order of crystallin proteins accounts for eye lens transparency

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cAMP-dependent phosphorylation of bovine lens alpha-crystallin

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The in vivo phosphorylation sites of bovine alpha B-crystallin

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Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology

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Structural properties of polydisperse biopolymer solutions: A light scattering study of bovine ?-crystallin

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Calf lens alpha-crystallin quaternary structure. A three-layer tetrahedral model

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A possible structure for alpha-crystallin

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Possible tetramer-based quaternary structure for alpha-crystallins and small heat shock proteins

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A possible chaperone-like quaternary structure for alpha-crystallin

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Computer-generated model of the quaternary structure of alpha crystallin in the lens

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Alpha-crystallin exists in a non-spherical form. A study on the rotational properties of native and reconstituted alpha-crystallin

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Further characterization of structural and electric properties of non-spherical alpha-crystallin

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Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin

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Alpha-crystallin can function as a molecular chaperone

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alpha B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues

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Expression of alpha B-crystallin in Alzheimer's disease.

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alpha m-Crystallin: the native form of the protein?

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Second virial coefficient of alpha-crystallin

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

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Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile

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EQUILIBRIUM ULTRACENTRIFUGATION OF DILUTE SOLUTIONS

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Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques

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A comparative study of the unfolding thermodynamics of vertebrate metmyoglobins

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Self-association of human and porcine relaxin as assessed by analytical ultracentrifugation and circular dichroism

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The crystal structure of the bacterial chaperonin GroEL at 2.8 A

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7 January 2021

10.1016/S0141-8130(98)00020-8

Identifiers

DOI

1 reference

6 February 2018

PubMed ID

9650077

1 reference

6 February 2018