Authors: Luisi, DL Raleigh, DP

Citation: Dl. Luisi et Dp. Raleigh, pH-dependent interactions and the stability and folding kinetics of the n-terminal domain of L9. Electrostatic interactions are only weakly formed inthe transition state for folding, J MOL BIOL, 299(4), 2000, pp. 1091-1100

Authors: Sato, S Luisi, DL Raleigh, DP

Citation: S. Sato et al., pH jump studies of the folding of the multidomain ribosomal protein L9: The structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain, BIOCHEM, 39(16), 2000, pp. 4955-4962

Authors: Luisi, DL Kuhlman, B Sideras, K Evans, PA Raleigh, DP

Citation: Dl. Luisi et al., Effects of varying the local propensity to form secondary structure on thestability and folding kinetics of a rapid folding mixed alpha/beta protein: Characterization of a truncation mutant of the N-terminal domain of the ribosomal protein L9, J MOL BIOL, 289(1), 1999, pp. 167-174

Authors: Luisi, DL Wu, WJ Raleigh, DP

Citation: Dl. Luisi et al., Conformational analysis of a set of peptides corresponding to the entire primary sequence of the n-terminal domain of the ribosomal protein L9: Evidence for stable native-like secondary structure in the unfolded state, J MOL BIOL, 287(2), 1999, pp. 395-407

Authors: Kuhlman, B Luisi, DL Young, P Raleigh, DP

Citation: B. Kuhlman et al., pK(a) values and the pH dependent stability of the N-terminal domain of L9as probes of electrostatic interactions in the denatured state. Differentiation between local and nonlocal interactions, BIOCHEM, 38(15), 1999, pp. 4896-4903

Authors: Kuhlman, B Luisi, DL Evans, PA Raleigh, DP

Citation: B. Kuhlman et al., Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9, J MOL BIOL, 284(5), 1998, pp. 1661-1670