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Brown MC, Mutter A, Koder RL, et al. Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy. J Raman Spectrosc. 2013;44(7):957-962doi: 10.1002/jrs.4316.
Brown, M. C., Mutter, A., Koder, R. L., JiJi, R. D., & Cooley, J. W. (2013). Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy. Journal of Raman spectroscopy : JRS, 44(7), 957-962. https://doi.org/10.1002/jrs.4316
Brown, Mia C, et al. "Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy." Journal of Raman spectroscopy : JRS vol. 44,7 (2013): 957-962. doi: https://doi.org/10.1002/jrs.4316
Brown MC, Mutter A, Koder RL, JiJi RD, Cooley JW. Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy. J Raman Spectrosc. 2013 Jul;44(7):957-962. doi: 10.1002/jrs.4316. Epub 2013 Jun 01. PMID: 27795611; PMCID: PMC5082991.
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J Raman Spectrosc. 2013 Jul;44(7):957-962. doi: 10.1002/jrs.4316. Epub 2013 Jun 01.

Observation of persistent α-helical content and discrete types of backbone disorder during a molten globule to ordered peptide transition via deep-UV resonance Raman spectroscopy.

Journal of Raman spectroscopy : JRS

Mia C Brown, Andrew Mutter, Ronald L Koder, Renee D JiJi, Jason W Cooley

Affiliations

  1. Department of Chemistry, University of Missouri, Columbia, MO 65211.
  2. Department of Physics, The City College of New York, New York, NY 10031.

PMID: 27795611 PMCID: PMC5082991 DOI: 10.1002/jrs.4316

Abstract

The molten globule state can aide in the folding of a protein to a functional structure and is loosely defined as an increase in structural disorder with conservation of the ensemble secondary structure content. Simultaneous observation of persistent secondary structure content with increased disorder has remained experimentally problematic. As a consequence, modeling how the molten globule state remains stable and how it facilitates proper folding remains difficult due to a lack of amenable spectroscopic techniques to characterize this class of partially unfolded proteins. Previously, deep-UV resonance Raman (dUVRR) spectroscopy has proven useful in the resolution of global and local structural fluctuations in the secondary structure of proteins. In this work, dUVRR was employed to study the molten globule to ordered transition of a model four-helix bundle protein, HP7. Both the average ensemble secondary structure and types of local disorder were monitored, without perturbation of the solvent, pH, or temperature. The molten globule to ordered transition is induced by stepwise coordination of two heme molecules. Persistent dUVRR spectral features in the amide III region at 1295-1301 and 1335-1338 cm

Keywords: dUVRR; deep-UV resonance Raman spectroscopy; molten globule; secondary structure; structural disorder; tertiary structure

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