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First‐principles calculations of protein circular dichroism in the far‐ultraviolet and beyond
Author(s) -
Oakley Mark T.,
Bulheller Benjamin M.,
Hirst Jonathan D.
Publication year - 2006
Publication title -
chirality
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.43
H-Index - 77
eISSN - 1520-636X
pISSN - 0899-0042
DOI - 10.1002/chir.20264
Subject(s) - circular dichroism , chemistry , folding (dsp implementation) , protein folding , spectroscopy , chirality (physics) , resolution (logic) , chemical physics , crystallography , nuclear magnetic resonance spectroscopy , nanosecond , stereochemistry , physics , optics , symmetry breaking , laser , quantum mechanics , biochemistry , artificial intelligence , computer science , electrical engineering , engineering , chiral symmetry breaking , nambu–jona lasinio model
Understanding the relationship between the amino acid sequence of a protein and its unique, compact three‐dimensional structure is one of the grand challenges in molecular biophysics. One exciting approach to the protein‐folding problem is fast time‐resolved spectroscopy in the ultra‐violet (UV). Time‐resolved electronic circular dichroism (CD) spectroscopy offers resolution on a nanosecond (or faster) timescale, but does not provide the spatial resolution of techniques like X‐ray crystallography or NMR. There is a need to underpin fast timescale spectroscopic studies of protein folding with a stronger theoretical foundation. We review some recent studies in this regard and briefly highlight how modern quantum chemical models of aromatic groups have improved the accuracy of calculations of protein CD spectra near‐UV. On the other side of the far‐UV, we describe calculations indicating that charge‐transfer transitions are likely to be responsible for bands observed in the vacuum UV in protein CD. Chirality 18:340–347, 2006. © 2006 Wiley‐Liss, Inc.