Tasayco's Group Publications

  1. On the NMR analysis of pKa values in the unfolded state of proteins by extrapolation to zero denaturant
    Quijada, J.; López, G.; Versace, R.; Ramírez, Luis; Tasayco, M. L.
    Biophysical Chemistry, in press.
  2. Magic Angle Spinning NMR Spectroscopy of Thioredoxin Reassemblies
    Jun, Y.; Sivakumar, P.; Cataldi, M.; Tasayco, M. L.; Polenova, T.
    Magnetic Resonance in Chemistry, submitted.
  3. The pH-dependence of amide chemical shift of Asp/Glu reflects its pKa in intrinsically disordered proteins with only local interactions
    Pujato, M.; Navarro, A.; Versace, R.; Mancusso, R.; Ghose, R.; Tasayco, M. L.
    Biochim. Biophys. Acta, 2006, 1764:1227-1233.
  4. Elucidating quantitative stability/flexibility relationships within thioredoxin and its fragments using a distance constraint model.
    Jacobs, D.; Livesay, D.; Hules, J.; Tasayco, M. L.
    J. Molec. Biology, 2006, 358:882-904.
  5. A selection for mutants that interfere with folding of E. coli thioredoxin in vivo.
    Huber, D.; Cha, M.-I.; Debarbieux, L.; Planson, A.; Cruz, N.; López, G.; Tasayco, M. L.; Chaffotte, A.; Beckwith, J.
    Proc. Natl. Acad. Sci. USA, 2005, 102:18872-18877.
  6. pH-Dependence of Amide Chemical Shifts in Natively Disordered Polypeptides Detects Medium-Range Interactions with Ionizable Residues.
    Pujato, M.; Bracken, C.; Mancusso, R.; Cataldi, M.; Tasayco, M. L.
    Biophysical Journal, 2005, 89:3293-3302.
  7. Resonance Assignments and Secondary Structure Analysis of E. coli Thioredoxin by Magic Angle Spinning Solid-State NMR Spectroscopy.
    Marulanda, D.; Tasayco, M. L.; Cataldi, M.; Arriarán, V.; Polenova, T.
    Journal of Physical Chemistry B, 2005, 109:18135-18145.
  8. Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. Resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.
    Marulanda, D.; Tasayco, M. L.; McDermott, A.; Cataldi, M.; Arriarán, V.; Polenova, T.
    JACS, 2004, 22:16608-16620.
  9. Reversal of negative charges on the surface of E. coli Thioredoxin: Pockets versus protrusions.
    Mancusso, R.; Cruz, E.; Cataldi, M.; Mendoza, C.; Fuchs, J.; Wang, H.; Yang, X.; Tasayco, M. L.
    Biochemistry, 2004, 43:3835-3843.
  10. Reduced spectral density mapping of a partially folded fragment of E. coli Thioredoxin.
    Daughdrill, G. W.; Vise, P. D.; Zhou, H.; Yang, X.; Yu, W.-F.; Tasayco, M. L.; Lowry, D.
    Journal of Biomolecular Structure and Dynamics, 2004, 21:663-670.
  11. DSC studies of a family of natively disordered fragments from Escherichia coli thioredoxin: Surface burial in intrinsic coils.
    Mendoza, C.; Figueirido, F.; Tasayco, M. L.
    Biochemistry, 2003, 42:3349-3358.
  12. Probing the structure and stability of a hybrid protein: The human E. coli thioredoxin chimera.
    Louis, J. M.; Georgescu, R. E.; Tasayco, M. L.; Tcherkasskaya, O.; Gronenborn, A. M.
    Biochemistry, 2001; 40:11184-11192.
  13. Heat capacity analysis of oxidized E. coli thioredoxin fragments (1-73, 74-108) and their non-covalent complex: Evidence for the burial of apolar surface in protein unfolded states.
    Georgescu, R. E.; García-Mira, M. D. M.; Tasayco, M. L.; Sánchez-Ruiz, J. M.
    European Biochemical Journal, 2001; 268:1477-1485.
  14. Interaction between two discontiguous chain segments from the β-sheet of E. coli thioredoxin suggests initiation site for folding.
    Tasayco, M. L.; Fuchs, J.; Yang, X.-M.; Dyalram, D.; Georgescu, R. E.
    Biochemistry, 2000; 39:10613-10618.
  15. NMR analysis of cleaved E. coli thioredoxin (1-73, 74-108) and its P76A variant: cis/trans peptide isomerization.
    Yu, W.-F.; Tung, C.-C.; Wang, H.; Tasayco, M. L.
    Protein Science 2000; 9:20-28.
  16. Energetics of assembling an artificial heterodimer with an α/β motif: Cleaved versus uncleaved E. coli thioredoxin.
    Georgescu, R. E.; Braswell, E. H.; Zhu, D.; Tasayco, M. L.
    Biochemistry 1999; 38:13355-13366.
  17. Recognition between disordered polypeptide chains from cleavage of an α/β domain: Self- versus non-self association
    Yang, X.-M.; Georgescu, R. E.; Li, J.-H.; Yu, W.-F.; Haierhan; Tasayco, M. L.
    Proceedings of the Pacific Symposium on Biocomputing 1999; 4: 590-600.
  18. NMR evidence for the reassembly of an α/β domain after cleavage of an α-helix: Implications for protein design.
    Yang, X.-M.; Yu, W.-F.; Li, J.-H.; Fuchs, J.; Rizo, J.; Tasayco, M. L.
    JACS 1998; 120(32): 7985-7986.
  19. Proline isomerization-independent accumulation of an early intermediate and heterogeneity of the folding pathways of a mixed α/β protein, Escherichia coli Thioredoxin.
    Georgescu, R. E.; Li, J.-H.; Goldberg, M. E.; Tasayco, M. L.; Chaffotte, A. F.
    Biochemistry. 1998 Jul 14; 37(28): 10286-10297.
  20. Recognition between disordered states: kinetics of the self-assembly of thioredoxin fragments.
    Chaffotte, A. F.; Li, J. H.; Georgescu, R. E.; Goldberg, M. E.; Tasayco, M. L.
    Biochemistry. 1997 Dec 23; 36(51): 16040-16048.
  21. NMR study of the reconstitution of the β-sheet of Thioredoxin by fragment complementation.
    Tasayco, M. L.; Chao, K.
    Proteins, 1995 May; 22(1): 41-44.