Allosteric effects in coiled-coil proteins folding and lanthanide-ion binding.
Peptide sequences modified with lanthanide-chelating groups at their N-termini, or at their lysine side chains, were synthesized, and new Ln(III) complexes were characterized. We show that partial folding of the conjugates to form trimer coiled coil structures induces coordination of lanthanides to the ligand, which in turn further stabilizes the 3D structure.
Department of Chemistry, Ben Gurion University of the Negev, Beer Sheva 84105, Israel.
Manickasundaram
M
Samiappan
Samaa
S
Alasibi
Rivka
R
Cohen-Luria
Abraham
A
Shanzer
Gonen
G
Ashkenasy
D000494:Allosteric Regulation; D001665:Binding Sites; D007477:Ions / Q000737:chemistry; D028581:Lanthanoid Series Elements / Q000737:chemistry*; D008024:Ligands; D049449:Luminescence; D008239:Lysine / Q000737:chemistry*; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000138:chemical synthesis* / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding
D007477:Ions; D028581:Lanthanoid Series Elements; D008024:Ligands; D009942:Organometallic Compounds; D010455:Peptides; D008239:Lysine