Using circular dichroism spectra to estimate protein secondary structure

By Norma J. Greenfield. Nature Protocols, 2007

3,727 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/9faad4ae77050184a4c9faf5f2efccea34708002

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In Materials Chemistry

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Citations in the corpus

Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions (2006, methodology): “An introduction to CD and a description of how to estimate the secondary structure of a protein from its CD spectrum are in the first protocol in this serie”
Sixty-five years of the long march in protein secondary structure prediction: the final stretch? (2016, background): “Typically, high-resolution X-ray structures [38–40] were extracted to build training and test sets for secondary structure prediction, although other experimental techniques such as nuclear magnetic resonance (NMR) chemical shifts [41, 42], circular dichroism spectra [43, 44] and infrared spectrosco”
Disorder Prediction Methods, Their Applicability to Different Protein Targets and Their Usefulness for Guiding Experimental Studies (2015, methodology): “CD is a rapid method for the classification of secondary structure of proteins in solution, based upon shifts in optical transitions, with structures defined by wavelength patterns [21].”
Accurate secondary structure prediction and fold recognition for circular dichroism spectroscopy (2015, background): “In the past decades, a multitude of enhanced algorithms, based on variable selection, or singular value decomposition of standardized, scaled, and calibrated reference spectra, have been proposed to predict the secondary structure content, with good overall secondary structure prediction (5, 6).”
DichroWeb, a website for calculating protein secondary structure from circular dichroism spectroscopic data (2021, background): “At present, only DichroWeb datasets 6 and 7, which each contain five spectra of denatured proteins (which may or may not be disordered in the same way as IDPs) specifically contain this type of structure.”
Structural and biophysical properties of FopA, a major outer membrane protein of Francisella tularensis (2022, neutral): “cm(2)/dmol was calculated as described [57].”