Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films.
TLDR
Attenuated total reflection Fourier-transform infrared spectroscopy of thin hydrated films of soluble and membrane protein included in a phospholipid bilayer is shown to provide useful information as to the secondary structure of the protein.Abstract:
Attenuated total reflection Fourier-transform infrared spectroscopy of thin hydrated films of soluble and membrane protein included in a phospholipid bilayer is shown to provide useful information as to the secondary structure of the protein. The analysis of the amide I band of deuterated samples by Fourier self-deconvolution followed by a curve fitting was performed by a new procedure in which all the input parameters are generated by the computer rather than by the investigator. The results of this analysis provide a correct estimation of the alpha-helix and beta-sheet structure content with a standard deviation of 8.6% when X-ray structures are taken as a reference. We also show that the orientation of the different secondary structures resolved by the Fourier self-deconvolution/curve-fitting procedure and of the phospholipid acyl chains can be simultaneously evaluated for membrane proteins reconstituted in a lipid bilayer. Of special interest for reconstitution of membrane proteins, the lipid/protein ratio can be accurately and quickly determined from the infrared spectrum.read more
Citations
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Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins.
Keh-Ming Pan,Michael J. Baldwin,J Nguyen,María Gasset,Ana Serban,Darlene Groth,Ingrid Mehlhorn,Ziwei Huang,Robert J. Fletterick,Fred E. Cohen +9 more
TL;DR: It is argued that the conversion of alpha-helices into beta-sheets underlies the formation of PrPSc, and it is likely that this conformational transition is a fundamental event in the propagation of prions.
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The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
TL;DR: This review critically assess the application of FTIR spectroscopy to the determination of protein structure by outlining the principles underlying protein secondary structure determination by FTIRSpectroscopy, and highlighting the situations in which FTIR Spectroscopy should be considered the technique of choice.
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Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment.
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Determining Beta-Sheet Crystallinity in Fibrous Proteins by Thermal Analysis and Infrared Spectroscopy
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References
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Examination of the secondary structure of proteins by deconvolved FTIR spectra.
D M Byler,H. Susi +1 more
TL;DR: Fourier transform ir (FTIR) spectra of 21 globular proteins have been obtained, revealing that the amide I band of each protein except casein consists of six to nine components, although all proteins do not exhibit components at every characteristic frequency.
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Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins.
Samuel Krimm,Jagdeesh Bandekar +1 more
TL;DR: The aim of this chapter is to present recent developments in the vibrational spectroscopy of peptides, polypeptides, and proteins.
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Three-dimensional model of purple membrane obtained by electron microscopy
Richard Henderson,P. N. T. Unwin +1 more
TL;DR: A 7-Å resolution map of the purple membrane has been obtained by electron microscopy of tilted, unstained specimens and shows that Lipid bilayer regions fill the spaces between the protein molecules.
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Internal Reflection Spectroscopy
N. J. Harrick,Joseph G. Hoffman +1 more
TL;DR: In this paper, it is shown that if the surface is flat and smooth, the nature of the reflection is called specular, i.e., mirror-like, and obeys the simple law that the angle of incidence equals the angles of reflection.
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