Control of metal coordination number in de novo designed peptides through subtle sequence modifications.
Substitution of an alanine for leucine (shown in light blue) in the hydrophobic interior of designed three-stranded coiled coils allows for the control of metal ion coordination number and geometry. The influence of this perturbation by a noncoordinating residue can be monitored by the dramatic impact on the 113Cd NMR spectrum. The structural effect occurs even when the residue substitution is as much as 7 A from the metal binding site.
Department of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, USA.
Kyung-Hoon
KH
Lee
Manolis
M
Matzapetakis
Soumya
S
Mitra
E Neil G
EN
Marsh
Vincent L
VL
Pecoraro
D000595:Amino Acid Sequence; D002104:Cadmium / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D007930:Leucine / Q000737:chemistry; D008667:Metalloproteins / Q000138:chemical synthesis / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*
D008667:Metalloproteins; D010455:Peptides; D002104:Cadmium; D007930:Leucine