List of Proteins
     
    Johnson (22) Johnson et al. (29) Keiderling and co-workers (5) Fasman and co-workers (13)
    Sreerama et al. (3 globular; 5 denatured)
    azurin myoglobin a-chymotrypsinogen reaction center  from Rhodopseudomonas viridis colicin A
    bence jones protein hemoglobin alcohol dehydrogenase photosystem I rat intestinal fatty acid binding protein
    a-chymotrypsin hemerythrin carbonic anhydrase reaction center from Rhodobacter sphaeroides green fluorescent protein
    concanavalin A T4 lysozyme glutathione reductase B 800-850 antenna complex from Rhodopseudomonas acidophila
    cytochrome C triose phosphate isomerase rhodanase ubiquinol-cytochrome c reductase from bovine heart Denatured Proteins (5)
    elastase lactate dehydrogenase
    cytochrome c oxidase from bovine heart apo-cytochrome C (5oC)
    flavodoxin lysozyme Yang and co-workers (6) rhodopsin from bovine retina apo-cytochrome C (90oC)
    hemerythrin thermolysin nuclease purple membrane from Halobacterium halobium ribonuclease (20oC)
    hemoglobin cytochrome C insulin Ca2+ ATPase from rabbit muscle sarcoplasmic reticulum staphyllococccal nuclease (6oC)
    lactate dehydrogenase phosphoglycerate kinase parvalbumin porin (gene OmpF product) from E. coli staphyllococccal nuclease (70oC)
    b-lactoglobulin EcoR1 endonuclease carboxypeptidase A porin from Rhodobacter capsulatus
    lysozyme flavodoxin bovine pancreatic trypsin inhibitor maltoporin (LamB)
    myoglobin subtilisin BPN adenylate kinase phosphoporin (PhoE)
    papain glyceraldehyde 3-p dehydrogenase


    pepsinogen papain


    prealbumin subtilisin novo


    ribonuclease A ribonuclease A


    superoxide dismutase pepsinogen


    T4 lysozyme beta-lactoglobulin


    thermolysin a-chymotrypsin


    triose phosphate isomerase azurin


    trypsin elastase



    g-crystallin



    prealbumin



    concanavalin A



    bence jones protein



    tumor necrosis factor



    superoxide dismutase



    a-bungarotoxin


References (PDF files of our papers are available here)
  1. Chen & Yang (1971) A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism.  Biochem Biophys Res Commun 44, 1285-1291.
  2. Chen et al. (1974) Determination of the helix and b-form of proteins in aqueous solution by circular dichroism.  Biochemistry 13, 3350-3359.
  3. Hennessey & Johnson (1981) Information Content in the Circular Dichroism of Proteins, Biochemistry, 20, 1085-1094.
  4. Provencher & Glockner (1981) Estimation of protein secondary structure from circular dichroism. Biochemstry. 20, 33-37.
  5. Compton & Johnson (1986) Analysis of Protein Circular Dichroism Spectra for secondary structures using a simple matrix Multiplication, Anal. Biochem., 155, 155-167.
  6. Yang et al. (1986). Calculation of protein conformation from circular  dichroism. Meth. Enzymol., 130, 208-269.
  7. Manavalan & Johnson (1987) Variable Selection Method improves the Prediction of Protein Secondary Structure from CD. Anal. Biochem., 167, 76-85.
  8. van Stokkum et al. (1990) Estimation of Protein Secondary Structure and Error Analysis from Circular Dichroism Spectra, Anal. Biochem., 191, 110-118.
  9. Pancoska & Keiderling (1991). Systematic comparison of statistical analysis of electronic and  vibrational circular dichroism for secondary structure prediction of selected proteins. Biochemistry,  30,  6885-6895.
  10. Sreerama & Woody (1993) A Self-Consistent Method for the analysis of Protein Secondary Structure from Circular Dichroism. Anal. Biochem., 209, 32-44.
  11. Sreerama & Woody (1994a) Poly(Pro)II helices in Globular Proteins: Identification and Circular Dichroic Analysis. Biochemistry, 33,10022-25.
  12. Sreerama & Woody (1994b) Protein secondary structure from circular dichroism spectroscopy. Combining variable selection principle and cluster analysis with neural network, ridge regression and self-consistent methods. J. Mol. Biol. 242:497-507.
  13. Sreerama et al. (1999) Estimation of the number of a-helical and b-strand segments in proteins using CD spectroscopy. Protein Science, 8, 370-380.
  14. Johnson (1999) Analyzing Protein CD for Accurate secondary Structures. Proteins: Str. Func. Genet., 35, 307-312.
  15. N. Sreerama, S.Y.Venyaminov and R.W. Woody. (2000) " Estimation of protein secondary structure from CD spectra: Inclusion of denatured proteins with native protein in the analysis" Anal. Biochem. 287, 243-251.
  16. N. Sreerama and R.W. Woody. (2000) "Estimation of protein secondary structure from CD spectra: Comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set" Anal. Biochem. 282, 252-260.
  17. N. Sreerama, S.Y.Venyaminov and R.W. Woody. (2001) "Analysis of protein CD spectra with a reference protein set based on tertiary structure class. Anal. Biochem. 299: 271-274.
  18. Sreerama N and R.W. Woody. (2004) On the analysis of membrane protein circular dichroism spectra Protein Science, 13, 100-112.
  19. Sreerama N and R.W. Woody. (2004) Computation and Analysis of  protein circular dichroism spectra Methods Enzymol, 383, 318. (Ch.13)..


Acknowledgements