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Results: 1-9 |
Results: 9

Authors: Alexandrescu, AT Snyder, DR Abildgaard, F
Citation: At. Alexandrescu et al., NMR of hydrogen bonding in cold-shock protein A and an analysis of the influence of crystallographic resolution on comparisons of hydrogen bond lengths, PROTEIN SCI, 10(9), 2001, pp. 1856-1868

Authors: Jaravine, VA Alexandrescu, AT Grzesiek, S
Citation: Va. Jaravine et al., Observation of the closing of individual hydrogen bonds during TFE-inducedhelix formation in a peptide, PROTEIN SCI, 10(5), 2001, pp. 943-950

Authors: Alexandrescu, AT Maciejewski, MW Ruegg, MA Engel, J Kammerer, RA
Citation: At. Alexandrescu et al., Letter to the Editor: H-1, C-13 and N-15 backbone assignments for the C-terminal globular domain of agrin, J BIOM NMR, 20(3), 2001, pp. 295-296

Authors: Kammerer, RA Jaravine, VA Frank, S Schulthess, T Landwehr, R Lustig, A Garcia-Echeverria, C Alexandrescu, AT Engel, J Steinmetz, MO
Citation: Ra. Kammerer et al., An intrahelical salt bridge within the trigger site stabilizes the GCN4 leucine zipper, J BIOL CHEM, 276(17), 2001, pp. 13685-13688

Authors: Jaravine, VA Rathgeb-Szabo, K Alexandrescu, AT
Citation: Va. Jaravine et al., Microscopic stability of cold shock protein A examined by NMR native statehydrogen exchange as a function of urea and trimethylamine N-oxide, PROTEIN SCI, 9(2), 2000, pp. 290-301

Authors: Alexandrescu, AT Lamour, FP Jaravine, VA
Citation: At. Alexandrescu et al., NMR evidence for progressive stabilization of native-like structure upon aggregation of acid-denatured LysN, J MOL BIOL, 295(2), 2000, pp. 239-255

Authors: Alexandrescu, AT Rathgeb-Szabo, K
Citation: At. Alexandrescu et K. Rathgeb-szabo, An NMR investigation of solution aggregation reactions preceding the misassembly of acid-denatured cold shock protein A into fibrils, J MOL BIOL, 291(5), 1999, pp. 1191-1206

Authors: Alexandrescu, AT Jaravine, VA Dames, SA Lamour, FP
Citation: At. Alexandrescu et al., NMR hydrogen exchange of the OB-fold protein LysN as a function of denaturant: The most conserved elements of structure are the most stable to unfolding, J MOL BIOL, 289(4), 1999, pp. 1041-1054

Authors: Dames, SA Kammerer, RA Moskau, D Engel, J Alexandrescu, AT
Citation: Sa. Dames et al., Contributions of the ionization states of acidic residues to the stabilityof the coiled coil domain of matrilin-1, FEBS LETTER, 446(1), 1999, pp. 75-80
Risultati: 1-9 |