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1). This Trp-zipper protein (denoted Trp-14) forms a stable pentameric coiled coil in solution. Its 1.45-Å crystal structure reveals an unprecedented interface ...
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We have applied this structure-sensitive tool to obtain detailed information on anchoring tryptophan residues in the β-barrel membrane protein, OmpA. Our ...
May 19, 2020 · Coiled-coils are α-helical structural protein motifs that wrap each other into supercoiled helices. They play essential roles as subunits that ...
Mar 3, 2023 · This perspective presents our current understanding of one class of protein assembly, the α-helical coiled coils. At first sight, these are ...
These coiled coils were designed and optimized to mimic features of the SNARE protein complex, involved in vesicle fusion processes [61], when tethered to lipid ...
Lipoprotein|Protein Folding|Coiled Coil|Pentamer|Tryptophan-Zipper|Membrane Protein from en.m.wikipedia.org
A coiled coil is a structural motif in proteins in which 2–7 alpha-helices are coiled together like the strands of a rope They have been found in roughly ...
Coiled-coil labeling is a simple, quick, and selective labeling method with moderate size for fluorescence imaging of live-cell membrane proteins. A robust ...
Lipoprotein|Protein Folding|Coiled Coil|Pentamer|Tryptophan-Zipper|Membrane Protein from www.nature.com
Jun 22, 2023 · Towards this aim, we selected the two-stranded antiparallel coiled coil as a domain fold that satisfies both criteria. A selection of ...
Sep 6, 2017 · Coiled coils are a robust motif for exploring amino acid interactions, generating unique supramolecular structures, and expanding the ...
Lipoprotein|Protein Folding|Coiled Coil|Pentamer|Tryptophan-Zipper|Membrane Protein from bmcecolevol.biomedcentral.com
Nov 16, 2005 · Here, we have identified all proteins with long coiled-coil domains from 21 additional fully sequenced genomes. Because regions predicted to ...