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Characterization of dry globular proteins and protein fibrils by synchrotron radiation vacuum UV circular dichroism

Characterization of dry globular proteins and protein fibrils by synchrotron radiation vacuum UV... Circular dichroism using synchrotron radiation (SRCD) can extend the spectral range down to ∼130 nm for dry proteins, potentially providing new structural information. Using a selection of dried model proteins, including α‐helical, β‐sheet, and mixed‐structure proteins, we observe a low‐wavelength band in the range 130–160 nm, whose intensity and peak position is sensitive to the secondary structure of the protein and may also reflect changes in super‐secondary structure. This band has previously been observed for peptides but not for globular proteins, and is compatible with previously published theoretical calculations related to π‐orbital transitions. We also show that drying does not lead to large changes in the secondary structure and does not induce orientational artifacts. In combination with principal component analysis, our SRCD data allow us to distinguish between two different types of protein fibrils, highlighting that bona fide fibrils formed by lysozyme are structurally more similar to the nonclassical fibrillar aggregates formed by the SerADan peptide than with the amyloid formed by α‐synuclein. Thus, despite the lack of direct structural conclusions, a comprehensive SRCD‐based database of dried protein spectra may provide a useful method to differentiate between various types of supersecondary structure and aggregated protein species. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 779–795, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biopolymers Wiley

Characterization of dry globular proteins and protein fibrils by synchrotron radiation vacuum UV circular dichroism

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References (66)

Publisher
Wiley
Copyright
Copyright © 2008 Wiley Periodicals, Inc., A Wiley Company
ISSN
0006-3525
eISSN
1097-0282
DOI
10.1002/bip.21011
pmid
18459170
Publisher site
See Article on Publisher Site

Abstract

Circular dichroism using synchrotron radiation (SRCD) can extend the spectral range down to ∼130 nm for dry proteins, potentially providing new structural information. Using a selection of dried model proteins, including α‐helical, β‐sheet, and mixed‐structure proteins, we observe a low‐wavelength band in the range 130–160 nm, whose intensity and peak position is sensitive to the secondary structure of the protein and may also reflect changes in super‐secondary structure. This band has previously been observed for peptides but not for globular proteins, and is compatible with previously published theoretical calculations related to π‐orbital transitions. We also show that drying does not lead to large changes in the secondary structure and does not induce orientational artifacts. In combination with principal component analysis, our SRCD data allow us to distinguish between two different types of protein fibrils, highlighting that bona fide fibrils formed by lysozyme are structurally more similar to the nonclassical fibrillar aggregates formed by the SerADan peptide than with the amyloid formed by α‐synuclein. Thus, despite the lack of direct structural conclusions, a comprehensive SRCD‐based database of dried protein spectra may provide a useful method to differentiate between various types of supersecondary structure and aggregated protein species. © 2008 Wiley Periodicals, Inc. Biopolymers 89: 779–795, 2008. This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

Journal

Biopolymers – Wiley

Published: Sep 1, 2008

Keywords: structural classes; protein films; band shift; hydration effects; orientational artifacts

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