Effects of temperature and concentration on bovine lens alpha-crystallin secondary structure: a circular dichroism spectroscopic study. (Q52260671)

28 April 2018

title

Effects of temperature and concentration on bovine lens alpha-crystallin secondary structure: a circular dichroism spectroscopic study. (English)

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28 April 2018

author name string

Farnsworth PN

1

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28 April 2018

Groth-Vasselli B

2

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Greenfield NJ

3

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28 April 2018

Singh K

4

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28 April 2018

publication date

1 July 1997

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28 April 2018

International Journal of Biological Macromolecules

published in

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28 April 2018

volume

20

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issue

4

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page(s)

283-291

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28 April 2018

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

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Some properties of the low molecular weight alpha-crystallin from normal human lens: comparison with bovine lens

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Structural homology of lens crystallins. III. Secondary structure estimation from circular dichroism and prediction from amino acid sequences

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Heat-induced changes in the conformation of α- and β-crystalline: Unique thermal stability of α-crystallin

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Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network.

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Variable selection method improves the prediction of protein secondary structure from circular dichroism spectra

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Information content in the circular dichroism of proteins.

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Interaction of ATP and lens alpha crystallin characterized by equilibrium binding studies and intrinsic tryptophan fluorescence spectroscopy

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Alpha-crystallins are involved in specific interactions with the murine gamma D/E/F-crystallin-encoding gene.

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Expression and aggregation of recombinant alpha A-crystallin and its two domains

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A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits.

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7 January 2021

Light scattering by bovine alpha-crystallin proteins in solution: hydrodynamic structure and interparticle interaction

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7 January 2021

An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure

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7 January 2021

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Identifiers

DOI

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28 April 2018

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28 April 2018