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. 1984 Mar;81(5):1406–1410. doi: 10.1073/pnas.81.5.1406

Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance

B A Wallace †, N Kohl †, M M Teeter ‡
PMCID: PMC344844  PMID: 16593429

Abstract

Crambin, a hydrophobic plant seed protein that exhibits sequence homology to membrane-active plant toxins, was incorporated into phospholipid vesicles. Circular dichroism spectroscopy indicates that its structure in vesicles is nearly identical to its structure in 60% ethanol solution, the solvent from which the protein was crystallized. The secondary structure predicted from the circular dichroism data of the ethanol solution closely resembles that determined by x-ray diffraction of the crystals. This agreement suggests that the x-ray structure may form a useful basis for modeling the structure and behavior of lipophilic plant toxins. Finally, because the structure of crambin has been determined in an organic solvent medium, it provides a protein standard for examination of the effect of solvent dipole moment on the circular dichroism spectra of proteins, which may be important for interpretation of data for membrane proteins.

Keywords: membrane proteins, secondary structure, plant toxins

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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