Authors:
Kuhlman, B
O'Neill, JW
Kim, DE
Zhang, KYJ
Baker, D
Citation: B. Kuhlman et al., Conversion of monomeric protein L to an obligate dimer by computational protein design, P NAS US, 98(19), 2001, pp. 10687-10691
Citation: B. Kuhlman et D. Baker, Native protein sequences are close to optimal for their structures (vol 97, pg 10383, 2000), P NAS US, 97(24), 2000, pp. 13460-13460
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
Citation: S. Sato et al., Folding of the multidomain ribosomal protein L9: The two domains fold independently with remarkably different rates, BIOCHEM, 38(17), 1999, pp. 5643-5650
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