Origin of the positive 225–230 nm circular dichroism band in proteins: Its application to conformational analysis

The 225–230 nm circular dichroism band found in many disulfide-containing proteins and peptides is sensitive to environmental changes. This band is assigned to the disulfide bond, the conformation of which influences both the intensity and λ max of the band. This property can be used to monitor subt...

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Bibliographic Details
Published in:Biophysical chemistry 1988-08, Vol.31 (1), p.45-51
Main Authors: Hider, R.C., Kupryszewski, G., Rekowski, P., Lammek, B.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Disulfide bond
Elapid Venoms
Models, Molecular
Oxytocin
Protein Conformation
Proteins
Spectrophotometry, Ultraviolet - methods
Toxin
Vasopressin
Vasopressins
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Summary:The 225–230 nm circular dichroism band found in many disulfide-containing proteins and peptides is sensitive to environmental changes. This band is assigned to the disulfide bond, the conformation of which influences both the intensity and λ max of the band. This property can be used to monitor subtle conformation changes observed in many polypeptides. Examples using the α-neurotoxins of elapid venoms and neurohypophyseal hormones are discussed.
ISSN:0301-4622
1873-4200
DOI:10.1016/0301-4622(88)80007-3