An antiparallel alpha-helical coiled-coil model system for rapid assessment of side-chain recognition at the hydrophobic interface.
Both parallel and antiparallel alpha-helical coiled-coil dimers are common among proteins; however, biophysical scrutiny has focused almost entirely on parallel dimers. We describe the development of a model system that enables efficient and systematic analysis of hydrophobic packing between antiparallel alpha-helices. Our findings reveal significant differences in packing preferences between parallel and antiparallel coiled-coils.
Hadley
Erik B
EB
Department of Chemistry, University of Wisconsin, Madison, WI 53706, USA.
Gellman
Samuel H
SH
D000595:Amino Acid Sequence; D019281:Dimerization; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D013816:Thermodynamics
D011506:Proteins