Resurrecting abandoned proteins with pure water: CD and NMR studies of protein fragments solubilized in salt-free water.

ABSTRACT: Many proteins expressed in Escherichia coli cells form inclusion bodies that are neither refoldable nor soluble in buffers. Very surprisingly, we recently discovered that all 11 buffer-insoluble protein fragments/domains we have, with a great diversity of cellular function, location, and molecular size, could be easily solubilized in salt-free water. The circular dichroism (CD) and NMR characterization led to classification of these proteins into three groups: group 1, with no secondary structure by CD and with narrowly-dispersed but sharp (1)H-(15)N heteronuclear single quantum correlation (HSQC) peaks; group 2, with secondary structure by CD but with HSQC peaks broadened and, consequently, only a small set of peaks detectable; and group 3, with secondary structure by CD and also well-sep

SUBMITTER: Li M 

PROVIDER: S-EPMC1635667 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature