Folding simulations of a de novo designed protein with a betaalphabeta fold.

ABSTRACT: betaalphabeta structural motifs are commonly used building blocks in protein structures containing parallel beta-sheets. However, to our knowledge, no stand-alone betaalphabeta structure has been observed in nature to date. Recently, for the first time that we know of, a small protein with an independent betaalphabeta structure (DS119) was successfully designed in our laboratory. To understand the folding mechanism of DS119, in the study described here, we carried out all-atom molecular dynamics and coarse-grained simulations to investigate its folding pathways and energy landscape. From all-atom simulations, we successfully observed the folding event and got a stable folded structure with a minimal root mean-square deviation of 2.6 A with respect to the NMR structure. The folding process

SUBMITTER: Qi Y 

PROVIDER: S-EPMC2808494 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature