Abstract
Empirical correlations have been made between protein vibrational circular dichroism (VCD) spectra for amide I and II modes and the fractions of secondary structure found in analyses of their X-ray crystal structure [1]. We have now studied protein VCD in another region, the amide III (primarily C-N stretch). Its measurement has proven difficult in the infrared due to its low overall absorbance intensity and to its mixing with other non-amide modes lying in the general region near 1300cm−1 [2].
This work funded by a grant from the National Institutes of Helth (GM3 1047).
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References
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Baello, B.I., Pancoska, P., Keiderling, T.A. (1997). Measurement of Amide III Vibrational Circular Dichroism of Proteins. In: Carmona, P., Navarro, R., Hernanz, A. (eds) Spectroscopy of Biological Molecules: Modern Trends. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-5622-6_11
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DOI: https://doi.org/10.1007/978-94-011-5622-6_11
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