Skip to main content
Sign In

University of Colorado Denver

​​​​​​​​​ ​
 

Protein Folding and Function: Dr. Mallela Research Laboratory

Publications


  1. R.L. Bis, S.M. Singh, J. Cabello-Villegas, and K.M.G. Mallela, Role of benzyl alcohol in the unfolding and aggregation of interferon alpha-2a, Journal of Pharmaceutical Sciences, In Press (2014). AbstractFull textPDF
  2. S.M. Singh, S. Bandi, D.D. Shah, G. Armstrong, and K.M.G. Mallela, Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function, PLoS One, 9 (2014) e110439. AbstractFull textPDF.
  3. R.L. Bis and K.M.G. Mallela, Antimicrobial preservatives induce aggregation of interferon alpha-2a: The order in which preservatives induce protein aggregation is independent of the protein, International Journal of Pharmaceutics, 472 (2014) 356-361. AbstractFull textPDF
  4. R.L. Bis, T.M. Stauffer, S.M. Singh, T.B. Lavoie, and K.M.G. Mallela, High yield soluble bacterial expression and streamlined purification of recombinant human interferon alpha-2a, Protein Expression and Purification, 99 (2014) 138-146. AbstractFull textPDF
  5. S. Bandi, S.M. Singh, and K.M.G. Mallela, The C-terminal domain of the utrophin tandem calponin-homology domain appears to be thermodynamically and kinetically more stable than the full-length protein, Biochemistry, 53 (2014) 2209-2211. AbstractFull TextPDF
  6. S.M. Singh, S. Bandi, S.J. Winder, and K.M.G. Mallela, The actin binding affinity of the utrophin tandem calponin-homology domain is primarily determined by its N-terminal domain, Biochemistry, 53 (2014) 1801-1809. AbstractFull TextPDF
  7. R.L. Hutchings, S.M. Singh, J. Cabello-Villegas, and K.M.G. Mallela, Effect of antimicrobial preservatives on partial protein unfolding and aggregation, Journal of Pharmaceutical Sciences, 102 (2013) 365-376. AbstractFull textPDF
  8. S.M. Singh and K.M.G. Mallela, The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin, Biophysical Journal, 103 (2012) 1970-1978. AbstractFull textPDF. Selected for a New & Notable: Biophysical Journal, 103 (2012) 1818-1819. Full textPDF
  9. S.M. Singh, J.F. Molas, N. Kongari, S. Bandi, G.S. Armstrong, S.J. Winder, and K.M.G. Mallela, Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin binding domains of utrophin and dystrophin, Proteins: Structure, Function, and Bioinformatics, 80 (2012) 1377-1392. AbstractFull textPDF
  10. S.M. Singh, R.L. Hutchings, and K.M.G. Mallela, Mechanisms of m-cresol induced protein aggregation studied using a model protein cytochrome c, Journal of Pharmaceutical Sciences, 100 (2011) 1679-1689. AbstractFull textPDF
  11. S.M. Singh, N. Kongari, J. Cabello-Villegas, and K.M.G. Mallela, Mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates, Proceedings of the National Academy of Sciences of the United States of America, 107 (2010) 15069-15074. AbstractFull textPDF
  12. S.M. Singh, J. Cabello-Villegas, R.L. Hutchings, and K.M.G. Mallela, Role of partial protein unfolding in alcohol-induced protein aggregation, Proteins: Structure, Function, and Bioinformatics, 78 (2010) 2625-2637. AbstractFull textPDF
  13. K.M.G. Mallela, Pharmaceutical Biotechnology – Concepts and Applications, Human Genomics, 4 (2010) 218-219. Full textPDF
  14. S. Bédard, M.M.G. Krishna, L. Mayne, and S.W. Englander, Protein folding: Independent unrelated pathways or predetermined pathway with optional errors, Proceedings of the National Academy of Sciences of the United States of America, 105 (2008) 7182-7187. (Equal contribution) AbstractFull textPDF
  15. S.W. Englander, L. Mayne, and M.M.G. Krishna, Protein folding and misfolding: Mechanism and principles, Quarterly Reviews of Biophysics, 40 (2007) 287-326. AbstractFull textPDF
  16. M.M.G. Krishna, H.Maity, J.N. Rumbley, and S.W. Englander, Branching in the sequential folding pathway of cytochrome c, Protein Science, 16 (2007) 1946-1956. AbstractFull textPDF
  17. M.M.G. Krishna and S.W. Englander, A unified mechanism for protein folding: Predetermined pathways with optional errors, Protein Science, 16 (2007) 449-464. AbstractFull textPDF 
  18. M.M.G. Krishna, H. Maity, J.N.Rumbley, Y. Lin, and S.W. Englander, Order of steps in the cytochrome c folding pathway: Evidence for a sequential stabilization mechanism, Journal of Molecular Biology, 359 ( 2006) 1410-1419. AbstractJournal coverFull textPDF
  19. R. Pidikiti, T. Zhang, K.M.G. Mallela, M. Shamim, K.S. Reddy, and J.S. Johansson, Sevoflurane-induced structural changes in a four-alpha-helix bundle protein, Biochemistry, 44 ( 2005) 12128-12135. AbstractFull textPDF
  20. R. Pidikiti, T. Zhang, K.M.G. Mallela, M. Shamim, K.S. Reddy, and J.S. Johansson, Structural changes in a four-alpha-helix bundle protein following sevoflurane binding, International Congress Series, 1283 ( 2005) 155-159. AbstractFull textPDF
  21. R. Pidikiti, M. Shamim, K.M.G. Mallela, K.S. Reddy, and J.S. Johansson, Expression and characterization of a four-alpha-helix bundle protein that binds the volatile general anesthetic halothane, Biomacromolecules, 6 ( 2005) 1516-1523. AbstractFull textPDF
  22. H. Maity, M. Maity, M.M.G. Krishna , L. Mayne, and S.W. Englander, Protein folding: The stepwise assembly of foldon units, Proceedings of the National Academy of Sciences of the United States of America, 102 (2005 ) 4741-4746. AbstractFull textPDF
  23. M.M.G. Krishna and S.W. Englander, The N-terminal to C-terminal motif in protein folding and function, Proceedings of the National Academy of Sciences of the United States of America, 102 ( 2005) 1053-1058. AbstractFull textPDF
  24. M.M.G. Krishna, Y. Lin, and S.W. Englander, Protein misfolding: Optional barriers, misfolded intermediates, and pathway heterogeneity, Journal of Molecular Biology, 343 ( 2004) 1095-1109. AbstractFull textPDF
  25. M.M.G. Krishna, L. Hoang, Y. Lin, and S.W. Englander, Hydrogen exchange methods to study protein folding, Methods, 34 ( 2004) 51-64. AbstractFull textPDF
  26. M.M.G. Krishna, Y. Lin, L. Mayne, and S.W. Englander, Intimate view of a kinetic protein folding intermediate: Residue-resolved structure, interactions, stability, folding and unfolding rates, homogeneity, Journal of Molecular Biology, 334 ( 2003) 501-513. AbstractFull textPDF
  27. L. Hoang, H. Maity, M.M.G. Krishna, Y. Lin, and S.W. Englander, Folding units govern the cytochrome c alkaline transition, Journal of Molecular Biology, 331 ( 2003) 37-43. AbstractFull textPDF
  28. M.M.G. Krishna, Y. Lin, J. Rumbley, and S.W. Englander, Cooperative omega loops in cytochrome c: Role in folding and function, Journal of Molecular Biology, 331 ( 2003) 29-36. AbstractFull textPDF
  29. L. Hoang, S. Bédard, M.M.G. Krishna, Y. Lin, and S.W. Englander, Cytochrome c folding pathway: Kinetic native-state hydrogen exchange, Proceedings of the National Academy of Sciences of the United States of America, 99 ( 2002) 12173-12178. AbstractFull textPDF
    Corrections: Proceedings of the National Academy of Sciences of the United States of America, 99 ( 2002) 15831. Full textPDF
  30. M.M.G. Krishna, Studying how a protein folds, The Alchemist (Web journal of chemweb.com), 2002. PDF
  31. S.W. Englander and M.M.G. Krishna, Hydrogen exchange, Nature Structural Biology, 8 ( 2001) 741-742. Full textPDF
  32. A.S.R. Koti, M.M.G. Krishna, and N. Periasamy, Time-resolved area-normalized emission spectroscopy (TRANES): A novel method for confirming emission from two excited states, Journal of Physical Chemistry A 105 ( 2001) 1767-1771. AbstractFull textPDF
  33. M.M.G. Krishna, A. Srivastava, and N. Periasamy, Rotational dynamics of surface probes in lipid vesicles, Biophysical Chemistry, 90 ( 2001) 123-133. AbstractFull textPDF
    Erratum: Biophysical Chemistry, 91 ( 2001) 209. Full textPDF
  34. A. Mishra, G.B. Behera, M.M.G. Krishna, and N. Periasamy, Time-resolved fluorescence studies of aminostyrylpyridinium dyes in organic solvents and surfactant micelles, Journal of Luminescence, 92 ( 2001) 175-188. AbstractFull textPDF
  35. M.M.G. Krishna, J. Samuel, and S. Sinha, Brownian motion on a sphere: Distribution of solid angles, Journal of Physics A: Mathematical and General, 33 ( 2000) 5965-5971. AbstractFull textPDF
    Also on ArXiv: http://arxiv.org/abs/cond-mat/0005345v3 PDF
  36. M.M.G. Krishna, R. Das, N. Periasamy, and R. Nityananda, Translational diffusion of fluorescent probes on a sphere: Monte Carlo simulations, theory and fluorescence anisotropy experiment, Journal of Chemical Physics, 112 ( 2000) 8502-8514. AbstractFull textPDF
  37. M.M.G. Krishna , Dynamics of Fluorescent Probes in Biological Systems, PhD Thesis, Tata Institute of Fundamental Research, University of Mumbai, India, 1999. PDF  © M.M.G. Krishna & N. Periasamy. Please cite the thesis when referring to unpublished results.
  38. M.M.G. Krishna and N. Periasamy, Location and orientation of DODCI in lipid bilayer membranes: Effects of lipid chain length and unsaturation, Biochimica et Biophysica Acta (Biomembranes), 1461 ( 1999) 58-68. AbstractFull textPDF
  39. M.M.G. Krishna, Excited state kinetics of the hydrophobic probe nile red in membranes and micelles, Journal of Physical Chemistry A, 103 ( 1999) 3589-3595. AbstractFull textPDF
    Additions and Corrections: Journal of Physical Chemistry A, 103 ( 1999) 4129. Full textPDF
    More Corrections: PDF
  40. M.M.G. Krishna and N. Periasamy, Orientational distribution of linear dye molecules in bilayer membranes, Chemical Physics Letters, 298 ( 1998) 359-367. AbstractFull textPDF
  41. M.M.G. Krishna, V.K. Rastogi, N. Periasamy, and K.V.R. Chary, Fluorescence and NMR studies on human seminal plasma prostatic inhibin: Association of lifetimes with sterically constrained tryptophans, Journal of Physical Chemistry B, 102 ( 1998) 5520-5528. AbstractFull textPDF
  42. M.M.G. Krishna and N. Periasamy, Fluorescence of organic dyes incorporated in lipid membranes: Site of solubilization and the effects of viscosity and refractive index on lifetimes, Journal of Fluorescence, 8 ( 1998) 81-91. AbstractFull textPDF
  43. N.C. Maiti, M.M.G. Krishna, P.J. Britto, and N. Periasamy, Fluorescence dynamics of dye probes in micelles, Journal of Physical Chemistry B, 101 ( 1997) 11051-11060. AbstractFull textPDF
  44. M.M.G. Krishna and N. Periasamy, Spectrally constrained global analysis of fluorescence decays in biomembrane systems, Analytical Biochemistry, 253 ( 1997) 1-7. AbstractFull textPDF

For comments, suggestions and complaints, please email Krishna.Mallela@ucdenver.edu.

The PDF files provided on this page are strictly for scientific, non-commercial research only. For all other purposes, the users should contact the respective copyright holders.