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A circular dichroic investigation of the secondary structure of lectins
Author(s) -
Herrmann M. S.,
Richardson C. E.,
Setzler L. M.,
Behnke W. D.,
Thompson R. E.
Publication year - 1978
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1978.360170906
Subject(s) - chemistry , lectin , protein secondary structure , aperiodic graph , concanavalin a , helix (gastropod) , dichroic glass , crystallography , spectral line , biochemistry , biology , physics , optics , combinatorics , mathematics , ecology , astronomy , snail , in vitro
The far‐uv CD spectra of eight lectins are presented. These eight lectins, as well as others previously studied, are grouped into three classes according to their particular CD spectra. The eight lectins studied appeared to have secondary structure dominated by β‐pleated sheet, which so far has been true of all lectins. An attempt was made to quantitate the three structural components (α‐helix, β‐pleated sheet, and aperiodic) in the lectins using the data for reference proteins given by Chen et al. [ Biochemistry 13 ,3350 (1974)]. For lectins in two of the classes, this method proved excellent and values for the three components are given. However, for the third class of lectins, which includes most of the lectins as well as Concanavalin A, this method of analysis proved to be unsatisfactory. This inadequacy was due to two factors: (1) the reference proteins used by Chen and (2) the unusual CD spectra of these lectins manifested by considerable ellipticity above 225 nm in a region where there are no known peptide electronic transitions.