2003
DOI: 10.1021/ja021464v
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Abstract: The vibrational Raman optical activity (ROA) spectrum of a polypeptide in a model beta-sheet conformation, that of poly(l-lysine), was measured for the first time, and the alpha-helix --> beta-sheet transition monitored as a function of temperature in H(2)O and D(2)O. Although no significant population of a disordered backbone state was detected at intermediate temperatures, some side chain bands not present in either the alpha-helix or beta-sheet state were observed. The observation of ROA bands in the extend… Show more

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Cited by 193 publications
(235 citation statements)
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“…It was previously stated that the only structure capable of fitting the constraints proposed by the EM data was a ␤-helix (24). Variations on the cylindrical ␤-sheet model proposed by Perutz et al (65) and on ␤-helix structures from soluble nonamyloid-forming proteins may be viable models with respect to the cross ␤-hydrogen bonding pattern; however, recent vibrational Raman optical activity experiments of reduced PrP conformers capable of fibrillization yield spectra similar to flat ␤-sheet proteins, not ␤-helix (66). Here, we have shown that a less complex conversion than that required for formation of a ␤-helix is observed directly by means of MD simulations and that the resulting converted conformation is capable of oligomerization into an analogously tightly packed protofibril in good agreement with the available experimental data.…”
Section: Discussionmentioning
confidence: 98%
“…It was previously stated that the only structure capable of fitting the constraints proposed by the EM data was a ␤-helix (24). Variations on the cylindrical ␤-sheet model proposed by Perutz et al (65) and on ␤-helix structures from soluble nonamyloid-forming proteins may be viable models with respect to the cross ␤-hydrogen bonding pattern; however, recent vibrational Raman optical activity experiments of reduced PrP conformers capable of fibrillization yield spectra similar to flat ␤-sheet proteins, not ␤-helix (66). Here, we have shown that a less complex conversion than that required for formation of a ␤-helix is observed directly by means of MD simulations and that the resulting converted conformation is capable of oligomerization into an analogously tightly packed protofibril in good agreement with the available experimental data.…”
Section: Discussionmentioning
confidence: 98%
“…Since then, hundreds of protein ROA spectra have been recorded and interpreted. It was soon apparent that, in addition to signatures of secondary structure like α-helix [76] and β-sheet [75], characteristic signals from loops and turns also appear which means that, rather than dwelling on ROA bands characteristic of secondary structure elements and how the corresponding percentages may be extracted, as is commonly done for other spectroscopic techniques, basic structural types or even motifs and folds in some cases might be recognized from the overall ROA band patterns. This is illustrated by the ROA spectra for a set of proteins with different folds displayed in Fig.…”
Section: Protein Structurementioning
confidence: 99%
“…An example of how protein ROA spectra contain motif or fold information is provided by the negative band at ∼1374 cm −1 assigned to β-turns in the ROA spectrum of the α + β protein bovine ribonuclease A in which the β-sheet is antiparallel: this band is absent from the ROA spectrum of the α/β protein subtilisin Carlsberg because the ends of the parallel β-strands within its Rossman fold are connected by extended α-helix sequences rather than by β-turns. Detailed vibrational band assignments are discussed elsewhere [9,11,20,26,75,76,105,106]. The large number of resolved structure-sensitive bands in protein ROA spectra makes them suitable for the application of multivariate analysis (pattern recognition) techniques to extract structural information.…”
Section: Protein Structurementioning
confidence: 99%
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“…[11] Transient vibrational spectroscopy has thus become a versatile tool for the investigation of reaction dynamics in solution, [12] often aided by reliable quantum chemistry calculations in the electronic ground state. The combination of experiment and theory is even more powerful in the case of chiral vibrational spectroscopies like vibrational circular dichroism (VCD) or Raman optical activity (ROA), by which it is possible to determine the absolute configuration of organic compounds in solution, [13][14][15][16] the conformation of polypeptides [17][18][19][20] or the secondary structure content of proteins. [19] Isotope labelling can be used to single out special regions of interest in larger molecules in order to obtain local structural information.…”
Section: Introductionmentioning
confidence: 99%