- Parallel folding pathways in the SH3 domain proteinA R Lam
Center for Polymer Studies, Department of Physics, Boston University, Boston, MA 02215, USA
J Mol Biol 373:1348-60. 2007..The finding motivates the hypothesis that the different experimentally observed TSEs in homologous proteins and circular permutants may represent potentially available pathways to the wild-type protein...
- Effects of the Arctic (E22-->G) mutation on amyloid beta-protein folding: discrete molecular dynamics studyA R Lam
Center for Polymer Studies, Physics Department, Boston University, Boston, Massachusetts 02215, USA
J Am Chem Soc 130:17413-22. 2008..Consequently, the N-terminal folded structure of the Arctic mutants closely resembles the N-terminal structure of Abeta42, suggesting that both Arctic Abeta peptides might assemble into structures similar to toxic Abeta42 oligomers...