Insight into polyproline II helical bundle stability in an antifreeze protein denatured state.

ABSTRACT: The use of polyproline II (PPII) helices in protein design is currently hindered by limitations in our understanding of their conformational stability and folding. Recent studies of the snow flea antifreeze protein (sfAFP), a useful model system composed of six PPII helices, suggested that a low denatured state entropy contributes to folding thermodynamics. Here, circular dichroism spectroscopy revealed minor populations of PPII like conformers at low temperature. To get atomic level information on the conformational ensemble and entropy of the reduced, denatured state of sfAFP, we have analyzed its chemical shifts and {¹H}-¹⁵N relaxation parameters by NMR spectroscopy at four experimental conditions. No significant populations of stable secondary structure were detec

SUBMITTER: Trevino MA 

PROVIDER: S-EPMC9748357 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature