Publications List from the Past Ten Years

Abstracts available for recent papers

  • Garai, K., Mustafi, S.M., Baban, B. and Frieden, C. (2009) Structural differences between apoli poprotein E3 and E4 as measured by (19)F- NMR Protein Sci, (E-pub ahead of print.) [Abstract]

  • Hu, X., Crick, S.L., Bu, G., Frieden, C., Pappu, R.V. and Lee, J.M. (2009) Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta paptide. PNAS, (E-pub ahead of print.) [Abstract]

  • Zhang, R., Hu, X., Khant, H., Ludtke, S.J., Chiu, W., Schmeid, M.F., Frieden, C. and Lee, J.M. (2009) Interprotofiliment interactions between Alzheimer's A{beta}1-42 peptides in amyloid fibrils revealed by cryoEM. PNAS, 103, 4653-4658.
  • Gerai, K., Crick, S.L., Mustafi, S.M. and Frieden, C. (2009) Expression and purification of amyloid-beta peptides from Escherichia coli Protein Expr Purif, 66, 107-112.
  • Frieden, C. (2008) A lifetime of kinetics J Biol Chem, 283, 19873-19878.

  • Frieden, C. (2007) Protein aggregation processes: In search of the mechanism. Protein Science, 16, 2334-2344.
  • Li, H. and Frieden, C. (2007) Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and 19F NMR. Proc Natl Acad Sci USA, 104, 11993-11998.
  • Li, H. and Frieden, C. (2007) Comparison of C40/82A and P27A C40/82A barstar mutants using 19F NMR Biochemistry, 46, 4337-4347.
  • Crick, S.L., Jayaraman, M., Frieden, C., Wetzel, R. and Pappu, R. (2006) Fluorescence correlation spectroscopy shows that monomeric polyglutamine molecules form collapsed structures in aqueous solutions. Proc Natl Acad Sci USA 103, 16764-16769.
  • Li, H. and Frieden, C. (2006) Fluorine-19 NMR studies on the acid state of the intestinal fatty acid binding protein Biochemistry 45, 6272-6278.
  • Chattopadhyay, K. and Frieden, C. (2006) Steady-state and time-resolved fluorescence studies of the intestinal fatty acid binding protein. Proteins 63 327-335.
  • Justice, S. S., Hunstad, D. A., Harper, J. R., Duguay, A. R., Pinkner, J. S., Bann, B., Frieden, C., Silhavy, T. J. and Hultgren, S. J. (2005) Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli J Bacteriol 187, 7680-7686.
  • Li, H. and Frieden, C. (2005) Phenylalanine side chain behavior of the intestinal fatty acid binding protein: The effect of urea on backbone and side chain stability. J Biol Chem 280, 38556-38561.
  • Chattopadhyay, K., Elson, E.L. and Frieden, C. (2005) The kinetics of conformational fluctuations in an unfolded protein measured by fluorescence methods. Proceedings of the National Academy of Sciences of the United States of America 102, 2385-2389.
  • Chattopadhyay, K., Saffarian, S., Elson, E.L. and Frieden, C. (2005) Measuring unfolding of proteins in the presence of denaturant using fluorescence correlation spectroscopy. Biophysical Journal 345, 599-610.
  • Li, H. and Frieden, C. (2005) NMR studies of 4-19f-phenylalanine-labeled intestinal fatty acid binding protein: Evidence for conformational heterogeneity in the native state. Biochemistry 44, 2369-2377.
  • Shu, Q. and Frieden, C. (2005) Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies J Mol Biol 345, 599-610.
  • Bann, J. G., Pinkner, J. S., Frieden, C. & Hultgren, S.J. (2004) Catalysis of protein folding by chaperones in pathogenic bacteria. Proceedings of the National Academy of Sciences of the United States of America 101, 17389-17393.
  • Bann, J.G. and Frieden, C. (2004) Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR. Biochemistry 43, 13775-13786.
  • Frieden, C., Hoeltzli, S.D. and Bann, J.G. (2004) The preparation of 19F-labeled proteins for NMR studies. Methods in Enzymology380, 400-415.
  • Shu, Q. and Frieden, C. (2004) Urea-dependent unfolding of murine adenosine deaminase: Sequential destabilization as measured by 19F NMR. 43, 1432-1439.
  • Nikiforovich, G.V, Andersen, N.H., Fesinmeyer, R.M. and Frieden, C. (2003) Possible locally driven folding pathways of TC5b, a 20-residue protein. Proteins 52, 292-302.
  • Frieden, C. (2003) The kinetics of side chain stabilization during protein folding. Biochemistry 42, 12439-12446.
  • Rajabzadeh M. Kao J and Frieden, C. (2003) Consequences of single-site mutations in the intestinal fatty acid binding protein. Biochemistry 42, 12192-12199.
  • Vorobiev, S., Strokopytov, B., Drubin, D.G., Frieden, C., Ono, S., Condeelis, J., Rubenstein, P.A. and Almo, S.C. (2003) The structure of nonvertebrate actin: Implications for the ATP hydrolytic mechanism. Proc. Natl. Acad. Sci. USA 100, 5760-5765.
  • Frieden, C., Chattopadhyay, K. and Elson, E.L. (2002) What fluorescence correlation spectroscopy can tell us about unfolded proteins. Advances in Protein Chemistry 62, 91-109.
  • Chattopadhyay, K. Saffarian, S., Elson, E.L. and Frieden, C. (2002) Measurement of microsecond dynamic motion in the intestinal fatty acid binding protein by using fluorescence correlation spectroscopy. Proc. Natl. Acad. of Sci. USA 99, 14171-14176.
  • Nikiforovich, G.V. and Frieden, C. (2002) The search for local native-like nucleation centers in the unfolded state of beta-sheet proteins. Proc. Natl. Acad. of Sci. USA 99, 10388-10393.
  • Nikoforovich, G.V. and Frieden, C. (2002) Molecular modeling study of the b-turn-type reversals involved in 3D structure of IFABP. in Peptides: The Wave of the Future. Eds. Lebl, M. and Houghton, R. A. Proc. of the American Peptide Society.

  • Chattopadhyay, K., Zhong, S., Yeh, S. R., Rousseau, D. L. and Frieden, C. (2002) The intestinal fatty acid binding protein: the role of turns in fast and slow folding processes. Biochemistry 41, 4040-4047.
  • J. G. Bann, J. Pinkner, S. J. Hultgren and C. Frieden. (2002) Real-time and equilibrium 19F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD. PNAS 99, 709-714.
  • J. G. Bann, S. W. Dodson, C. Frieden and S. J. Hultgren. (2002) Adhesive pili of the chaperone-usher family. "In Pathogenic E. Coli: Paradigm of bacterial pathogenesis." Ed. M. Donnenberg, Academic Press, San Diego.

  • C. Frieden, E. S. Huang and J. W. Ponder. (2001) Turn Scanning: experimental and theoretical approaches to the role of turns. In "Protein Structure, Stability and Folding" 2nd Ed. K. Murphy, Ed. Humana Press. pp.133-158

  • M. E. Hodsdon and C. Frieden. (2001) Intestinal fatty acid binding protein: The folding mechanism as determined by NMR studies. Biochemistry 40, 732-742.
  • M. M. Barnhart, J. S. Pinkner, G. E. Soto, F. G. Sauer, S. Langermann, G. Waksman, C. Frieden and S. J. Hultgren. (2000) PapD-like Chaperones Provide the Missing Information for Folding of Pilin Proteins. Proc. Natl. Acad. Sci. 97, 7709-7714.

  • C. Frieden, J. Du, L. Schriefer, and J. Buzan. (2000) Purification and Polymerization Properties of Two Lethal Actin Mutants. Biochem. Biophys. Res. Communs. 271, 464-468.
  • A. C. Clark, B. S. Karon, and C. Frieden. (1999) Cooperative effects of potassium, magnesium, and magnesium-ADP on the release of Escherichia coli dihydrofolate reductase from the chaperonin GroEL. Protein Science 8, 2166-2176.
  • J. Buzan, J. Du, T. Karpova, and C. Frieden. (1999) Histidine-tagged wild-type yeast actin: Its properties and use in a novel approach for obtaining yeast actin mutants. Proc. Natl. Acad. Sci. USA 96, 2823-2827.
  • A. C. Clark and C. Frieden. (1999) Native E. coli and murine dihydrofolate reductases contain late folding non-native structures. J. Mol. Biol. 285, 1765-1776.
  • A. C. Clark and C. Frieden. (1999) The chaperonin GroEL binds to late folding non-native conformations present in native E. coli and murine dihydrofolate reductases. J. Mol. Biol. 285, 1777-1788.