CORRELATE WELL (R = )0.97) WITH THE MEASURED HELICITY OF EACH DIM...

2010) - BÁO CÁO KHOA HỌC: THERMODYNAMIC ANALYSIS OF JUN–FOS COILED COIL PEPTIDE ANTAGONISTS PDF
Khoa học BÁO CÁO KHOA HỌC: THERMODYNAMIC ANALYSIS OF JUN–FOS COILED COIL PEPTIDE ANTAGONISTS PDF
2010)

correlate well (r = )0.97) with the measured helicity of each dimeric pair.

The more helical the antagonist–target complex, the more favourable the

doi:10.1111/j.1742-4658.2010.07988.x

change in enthalpy, which is in turn opposed more strongly by entropy.

Antagonistic peptides are predicted to represent excellent scaffolds for fur-

ther refinement. By contrast, the wild-type cJun–cFos complex is domi-

nated by a favourable entropic contribution, owing partially to a decrease

in buried hydrophobic groups from cFos core residues and an increase in

the conformational freedom.

Structured digital abstract

l

MINT-8077649,MINT-8077677,MINT-8077771,MINT-8077789,MINT-8077811,MINT-