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Average orientation of aromatic residues in proteins determined from linear dichroism spectroscopy. A comparison of results on bovine gamma-crystallins with X-ray data.

Abstract：

:The structures of the two very closely related proteins, bovine gamma II- and gamma IVa-crystallin have been studied by means of near-ultra-violet linear dichroism spectroscopy on squeezed polyacrylamide gel systems. The crystallin spectra are discussed in terms of the spectra of the aromatic chromophores present in these proteins and provide detailed information on the average orientation of these residues in the proteins. A comparison of our results with information based on crystallographic X-ray experiments shows excellent agreement, reflecting even some of the minor differences between the two proteins studied. Since linear dichroism measurements as performed here take a few days only, and can be done on most aqueous protein solutions, linear dichroism spectroscopy may give a valuable contribution to structural studies on proteins.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Bloemendal M,Leunissen JA,van Amerongen H,van Grondelle R

doi

10.1016/s0022-2836(05)80069-5

subject

Has Abstract

pub_date

1990-11-05 00:00:00

pages

181-6

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)80069-5

journal_volume

216

pub_type

杂志文章

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