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Wallace BA, Kohl N, Teeter MM. Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance. Proc Natl Acad Sci U S A. 1984;81(5):1406-10doi: 10.1073/pnas.81.5.1406.
Wallace, B. A., Kohl, N., & Teeter, M. M. (1984). Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance. Proceedings of the National Academy of Sciences of the United States of America, 81(5), 1406-10. https://doi.org/10.1073/pnas.81.5.1406
Wallace, B A, et al. "Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance." Proceedings of the National Academy of Sciences of the United States of America vol. 81,5 (1984): 1406-10. doi: https://doi.org/10.1073/pnas.81.5.1406
Wallace BA, Kohl N, Teeter MM. Crambin in phospholipid vesicles: Circular dichroism analysis of crystal structure relevance. Proc Natl Acad Sci U S A. 1984 Mar;81(5):1406-10. doi: 10.1073/pnas.81.5.1406. PMID: 16593429; PMCID: PMC344844.
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Proc Natl Acad Sci U S A. 1984 Mar;81(5):1406-10. doi: 10.1073/pnas.81.5.1406.

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

Proceedings of the National Academy of Sciences of the United States of America

B A Wallace, N Kohl, M M Teeter

Affiliations

  1. Department of Biochemistry, Columbia University, New York, NY 10032.

PMID: 16593429 PMCID: PMC344844 DOI: 10.1073/pnas.81.5.1406

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.

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