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Using the additional parameters from the second derivative spectra for lysozyme Figure , the resulting peak number is 6.

1. Biomolecules in the gas phase

The Table compares the secondary structure contents for different techniques with results from X-ray crystallography. Levitt et al.

J Mol Biol Aug 5; 2 b F. Eisenhaber et al. Luo et al. Anal Biochem Jan; 1 Using the parameters a0, a1 and a2, the secondary structure content derived from FTIR spectra is in agreement with X-ray crystallography data. The structural components were quantified by the integrated areas of the respective peaks.

This implies that the effective absorptivities can be assumed to be equal. Circular Dichroism CD spectroscopy is a well established technique for the analysis of secondary structure of proteins in aqueous solution. This technique seems to be less reliable for the study of aggregated proteins, inclusion bodys or membrane bound proteins due to light scattering problems associated with large membrane fragments or aggregates.

FTIR spectroscopy has proved to be a powerful tool for investigations on proteins discussed above.

Encyclopedia of Spectroscopy and Spectrometry

The second derivatives of all spectra were calculated using the spectrometer software OPUS. Before starting the fitting procedure, the obtained depths of the minima in the second derivative spectrum and, subsequently, the calculated maximum intensities were corrected for the interference of all neighboring peaks. The curve fitting is performed by stepwise iterative adjustment towards a minimum root-mean-square error of the different parameters determining the shape and position of the absorption peaks.

The data reveal that the amide I band for all proteins consists of six or seven major components which were found in all spectra. The helix content derived from the amide I region for lysozyme, lactate dehydrogenase and citrate synthase is in agreement with the data from X-ray crystallography.

The helix content in the FAB fragment of mouse antibody is too low, the beta-sheet content too high. Visual inspection of the amide I envelope of the native and thermally denatured states revealed a striking difference in the band shapes. For the native state, the band is fairly asymmetric and has a peak maximum around cm -1 which corresponds to alpha-helical structure. In contrast, the denatured proteins show an additional maximum between and cm -1 , indicative of the predominance of beta-sheet and unordered structures. In the following afew papers applying FTIR spectroscopy to denatured proteins and inclusion bodies are compiled.

J Biol Chem Sep 30; 39 , Sancho et al. Biochemistry Jan 24;34 3 , Menendez et al. Eur J Biochem Dec 15; 3 , Boye et al. J Dairy Res Feb;63 1 , Xie et al.


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Arch Biochem Biophys Apr 1; 1 , Bramanti et al. Biopolymers May;38 5 , Biopolymers Aug;42 2 , Jiang et al. Biochim Biophys Acta May 23; 2 , Lee et al. Biomaterials Aug;17 16 , Azuaga et al. Biochemistry Dec 17;35 50 , Narhi et al. J Pept Res Oct;50 4 , Magdaleno et al.

Science Feb 20; , Tablin et al. J Cell Physiol Aug; 2 , Oberg et al. Biochemistry Mar 8;33 9 Hetero DB. Site DB. Classification Trees. Entry Lists. E-mail: info leibniz-fli. For peptides, the structural issue is not one of the configuration, but of conformation, and the flexibility of the oligomeric structure raises major computational challenges.

Circular dichroism spectroscopy

Turns are a vital aspect of peptide and protein conformation that allow such structures to fold into a compact unit. However, unlike helices and sheets, they are not extended repeating structures, but each residue has a different local conformation. Also, when turns are part of larger peptides their termini are connected to completely different structural elements. We have done extended comparative density functional theory DFT computations to characterize the expected spectral contributions of selected turn structures to the amide IR and VCD spectra of peptides.


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The isolated vacuum results for tri-amide turns Ac-X-Y-NH 2 of a few different sequences are compared with calculations involving correction for solvation effects. The nature of some turn-associated, amide originating, spectral transitions are developed and tested. Unable to display preview. Download preview PDF. Skip to main content. Advertisement Hide.

Infrared Analysis of Peptides and Proteins: Principles and Applications

DFT-based study of infrared absorption and vibrational circular dichroism for various conformers including solvent effects. Regular Article First Online: 22 December This is a preview of subscription content, log in to check access. Wiley-Liss, Chichester Google Scholar. Barth A, Zscherp C ACS Symposium Series.

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Biochemistry CrossRef Google Scholar. Keywords: x-ray crystallography, nuclear magnetic resonance, circular dichroism, fluorescence, infrared and raman spectroscopies, mass spectrometry, aromatic moieties, proteins, peptides. Abstract: To perform its biochemical functions, a protein usually folds into a well defined, highly ordered structure. Journal Name: Current Organic Chemistry.

Introduction

Volume 7 , Issue 18 , Journal Home. Keywords: x-ray crystallography, nuclear magnetic resonance, circular dichroism, fluorescence, infrared and raman spectroscopies, mass spectrometry, aromatic moieties, proteins, peptides Abstract: To perform its biochemical functions, a protein usually folds into a well defined, highly ordered structure. Close Print this page.