Simulated annealing was performed to model parallel dimers of α-helical transmembrane
peptides with the sequence L11XL12, predicting left-handed coiled coil geometry in all …

The forces contributing to the association of transmembrane helices in folded membrane
proteins have received considerable attention recently. In this study we investigate the …

Membrane‐embedded protein domains frequently exist as α‐helical bundles, as exemplified
by photosynthetic reaction centers, bacteriorhodopsin, and cytochrome C oxidase. The …

Recent studies with model peptides and statistical analyses of the crystal structures of
membrane proteins have shown that buried polar interactions contribute significantly to the …

The forces that define the interactions of transmembrane helices have been evaluated using
a model membrane-soluble peptide (MS1), whose packing is modeled on the two-stranded …

The prediction and design at the atomic level of membrane protein structures and
interactions is a critical but unsolved challenge. To address this problem, we have …

Within 1 or 2 decades, the reputation of membrane‐spanning α‐helices has changed
dramatically. Once mostly regarded as dull membrane anchors, transmembrane domains …

TMDOCK is a novel computational method for the modeling of parallel homodimers formed
by transmembrane (TM) α-helices. Three-dimensional (3D) models of dimers are generated …

An understanding of structure–function relationships of membrane proteins continues to be
a challenging problem, owing to the difficulty in obtaining their structures experimentally …

Recent experiments and analysis have demonstrated the important roles of hydrogen
bonding and polar–polar interactions in driving transmembrane helix–helix association …