Narasimha Sreerama
Department of Biochemistry & Molecular Biology, 
Colorado State University,
Fort Collins, CO 80523, USA. 
Tel: (970) 491-0436(work) 
Fax: (970) 491-0494 
E-mail: Narasimha.Sreerama@colostate.edu 
My research interests are in the general area of protein structure, molecular modeling and biomolecular spectroscopy. The application of  circular dichroism (CD) spectroscopy to protein and nucleic acid structure forms the major part of my research. We have developed methods to obtain protien structural informaiton (secondary structure fractions, number of alpha-helical and beta-strand segments, and the tertiary structure class) from CD spectra and, conversely, to compute CD spectrum from the three-dimensional structure of protien. We have also developed methods to compute the CD spectra of nucleic acids from A, B, and Z conformations. Our future research includes the inclusion of the CD-derived structural information in predicting protein strucutre and modeling denatured protiens.

Our computer software package CDPro includes three programs for protein CD analysis, seven to eight reference protein sets, one program for tertiary structure class determination. The latest addition to CDPro is the inclusion of membrane protien CD spectra in the existing soluble protien reference sets.

Selected Publications
  1. N. Sreerama and R.W. Woody. (2004) Computation and Analysis of Protein Circular Dichroism Spectra. Meth. Enzymol. (in press). PDF File
  2. N. Sreerama and R.W. Woody. (2004) On the analysis of membrane protein circular dichroism spectra. Protein Sci. (in Press). PDF File
  3. N. Sreerama and R.W. Woody. (2003) Structural Composition of beta-I and bete-II Proteins. Protein Sci. 12, 384-388. PDF_File
  4. C. Kiefl, N. Sreerama, R. Haddad, L. Sun,  W. Jentzen, Y. Lu, Y. Qiu, J.A. Shelnutt, and R.W. Woody, (2002) Heme Distortions in Sperm-Whale Carbonmonoxy Myoglobin: Correlations between Rotational Strengths and Heme Distortions in MD-Generated Structures. J. Am. Chem. Soc. 124, 3385-3394. PDF_File
  5. 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. PDF_File
  6. Y. Griko, N. Sreerama, P. Osumi-Davis, R.W. Woody and A-Y.W. Woody. (2001) Thermal and urea-induced unfolding in T7 RNA polymerase: Calorimetry, Circular Dichroism and Fluorescence study. Prot. Sci. 10, 845-853. PDF_File
  7. 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. PDF_File
  8. N. Sreerama, S.Y.Venyaminov and R.W. Woody. (1999) Estimation of the number of alpha-helical and beta-sheet segments in proteins using circular dichroism spectroscopy.  Protein Science, 8, 370. PDF_File
  9. R.W. Woody and N. Sreerama. (1999) Comment on ‘Improving protein circular dichroism calculations in the far-ultraviolet through reparameterizing the amide chromophore’ [J. Chem. Phys. 109, 782 (1998)]. J. Chem. Phys. 111,  2844. PDF_File
  10. N. Sreerama, M.C. Manning, ME. Powers, D.M. Goldenberg and R.W. Woody. (1999) Tyrosine, phenylalanine and disulfide contributions to the protein circular dichroism spectra: CD spectra of wild-type and mutant BPTI. Biochemistry 38, 10814-10822. PDF File
  11. N. Sreerama and R.W. Woody. (1999) Molecular dynamics simulations of polypeptide conformations in water: A comparison alpha, beta and poly(Pro)II structures. Proteins: Struc. Func. Genet. 36, 400. PDF_File
  12. N. Sreerama and R.W. Woody (1994) Poly(Pro)II type structure in globular proteins - Identification and CD analysis. Biochemistry, 33, 10022. PDF_File
  13. N. Sreerama and R.W. Woody (1993) A self consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochemistry, 209, 32. PDF_File

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