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. 1987 Jun;84(12):4113–4116. doi: 10.1073/pnas.84.12.4113

Structural basis of human erythrocyte glucose transporter function in proteoliposome vesicles: circular dichroism measurements.

J J Chin, E K Jung, V Chen, C Y Jung
PMCID: PMC305033  PMID: 3473495

Abstract

The secondary structural compositions of the human erythrocyte glucose transporter in proteoliposome vesicles were assessed on the basis of circular dichroism (CD) spectra measured in the absence and in the presence of D-glucose or an inhibitor, cytochalasin B. We designed and used a scattered-light-collecting device, which corrects CD spectra for optical artifacts originating from light scattering. Relative contents of eight types of secondary structure were estimated by using basis spectra generated by the eigenvector method based on CD spectra of 15 proteins of known structure. Results indicate that the glucose transporter is composed of approximately 82% alpha-helices, 10% beta-turns, and 8% other random structure, with no beta-strands. In the presence of an excess of D-glucose, the alpha-helical content is reduced by more than 10% and there is a significant increase in the random structure content. Cytochalasin B does not appear to affect the secondary structural composition of the transporter to any significant degree.

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Selected References

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