Circular dichroism spectroscopy has intrinsic limitations for protein secondary structure analysis

Analytical Biochemistry

Volumn 389, Issue 2, 2009, Pages 174-176

  Khrapunov, Sergei ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DICHROISM; PROTEINS;

BETA-STRAND; CD SPECTRA; CIRCULAR DICHROISM SPECTRA; PROTEIN SECONDARY STRUCTURE; SECONDARY STRUCTURES; THREE-DIMENSIONAL STRUCTURE;

CIRCULAR DICHROISM SPECTROSCOPY;

PROTEIN;

ARTICLE; CALCULATION; CIRCULAR DICHROISM; GEOMETRY; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE;

EID: 67349104401     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2009.03.036     Document Type: Article

References (16)

1. Greenfield N. Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. 1 (2006) 2876-2880
2. Greenfield N. Determination of the folding of proteins as a function of denaturants, osmolytes, or ligands using circular dichroism. Nat. Protoc. 1 (2006) 2733-2741
3. Greenfield N. Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 1 (2006) 2876-2890
4. Sreerama N., and Woody R. Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
5. Whitmore L., and Wallace B. DICHROWEB, An online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32 (2004) W668-W673
6. Sreerama N., Venyaminov S., and Woody R. Estimation of the number of α-helical and β-strand using circular dichroism spectroscopy. Protein Sci. 8 (1999) 370-380
7. Sreerama N., Venyaminov S., and Woody R. Analysis of protein circular dichroism spectra based on the tertiary structure classification. Anal. Biochem. 299 (2001) 271-274
8. Matsuo K., Yonehara R., and Gekko K. Improved estimation of the secondary structures of proteins by vacuum-ultraviolet circular dichroism spectroscopy. J. Biochem. 138 (2005) 79-88
9. Wallace B., Lees J., Orry A., Lobley A., and Janes R. Analyses of circular dichroism spectra of membrane proteins. Protein Sci. 12 (2003) 875-884
10. Levitt M., and Chotia C. Structural patterns in globular proteins. Nature 261 (1976) 552-558
11. Manalavan P., and Johnson W.J. Sensitivity of circular dichroism to protein tertiary structure class. Nature 305 (1983) 831-832
12. Grudzielanek S., Jansen R., and Winter R. Solvational tuning of the unfolding, aggregation, and amyloidogenesis of insulin. J. Mol. Biol. 351 (2005) 879-894
13. Sreerama N., and Woody R. Computation and analysis of protein circular dichroism spectra. Methods Enzymol. 383 (2004) 318-351
14. Khrapunov S., Cheng H., Hegde S., Blanchard J., and Brenowitz M. Solution structure and refolding of the mycobacterium tuberculosis pentapeptide repeat protein MfpA. J. Biol. Chem. 283 (2008) 36290-36299
15. Janes R. Bioinformatics analysis of circular dichroism protein reference databases. Bioinformatics 21 (2005) 4230-4238
16. Wallace B., Lee W., and Janes R. The Protein Circular Dichroism Data Bank (PCDDB): A bioinformatics and spectroscopic resource. Proteins 62 (2006) 1-3