Bovine lens crystallins do contain helical structure: a circular dichroism study. (Q52209301)

27 April 2018

title

Bovine lens crystallins do contain helical structure: a circular dichroism study. (English)

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27 April 2018

author name string

M Bloemendal

series ordinal

1

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27 April 2018

A Toumadje

series ordinal

2

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27 April 2018

W C Johnson

series ordinal

3

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27 April 2018

publication date

1 July 1999

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27 April 2018

Biochimica et Biophysica Acta

published in

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27 April 2018

volume

1432

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27 April 2018

issue

2

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27 April 2018

page(s)

234-238

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27 April 2018

https://api.crossref.org/works/10.1016%2FS0167-4838%2899%2900107-7

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The conformation of eye-lens proteins studied by means of optical rotatory dispersion

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Estimation of the secondary structure and conformation of bovine lens crystallins by infrared spectroscopy: quantitative analysis and resolution by Fourier self-deconvolution and curve fit.

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Biochemical characterization of crystallins from frog lenses

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X-ray analysis of the eye lens protein gamma-II crystallin at 1.9 A resolution

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X-ray analysis of beta B2-crystallin and evolution of oligomeric lens proteins

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High resolution structure of an oligomeric eye lens beta-crystallin. Loops, arches, linkers and interfaces in beta B2 dimer compared to a monomeric gamma-crystallin

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

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alpha-Crystallin C-terminal domain: on the track of an Ig fold

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Estimation of globular protein secondary structure from circular dichroism.

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Estimation of protein secondary structure and error analysis from circular dichroism spectra

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Quantitative analysis of protein far UV circular dichroism spectra by neural networks

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Methods to estimate the conformation of proteins and polypeptides from circular dichroism data

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Extending CD spectra of proteins to 168 nm improves the analysis for secondary structures

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The isolation of lens crystallins using lens liquid as the solvent

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The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II

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Information content in the circular dichroism of proteins.

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Lens alpha-crystallin: chaperone-like properties

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A critical evaluation of methods for prediction of protein secondary structures

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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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Identifiers

DOI

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27 April 2018

1 reference

27 April 2018