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Coiled-Coil Domain

Known as: Coiled-Coil, 4-3 Hydrophobic Repeat, Left-Handed Twist 
A domain that stabilizes alpha helices in proteins through a very efficient burial of hydrophobic side chains so that polar water molecules do not… Expand
National Institutes of Health

Papers overview

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Review
2017
Review
2017
Lipids are essential building blocks synthesized by complex molecular pathways and deposited as lipid droplets (LDs) in cells… Expand
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Highly Cited
2006
Highly Cited
2006
We introduce Paircoil2, a new version of the Paircoil program, which uses pairwise residue probabilities to detect coiled-coil… Expand
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Review
2004
Review
2004
The coiled coil is a common structural motif, formed by approximately 3 ± 5% of all amino acids in proteins. Typically, it… Expand
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Review
2001
Review
2001
The alpha-helical coiled coil is one of the principal subunit oligomerization motifs in proteins. Its most characteristic feature… Expand
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Highly Cited
1997
Highly Cited
1997
A new multidimensional scoring approach for identifying and distinguishing trimeric and dimeric coiled coils is implemented in… Expand
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Review
1996
Review
1996
Over the past five years, the structures of more than 20 proteins containing coiled-coil domains have been solved to high… Expand
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Highly Cited
1993
Highly Cited
1993
Coiled-coil sequences in proteins consist of heptad repeats containing two characteristic hydrophobic positions. The role of… Expand
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Highly Cited
1991
Highly Cited
1991
The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking… Expand
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Highly Cited
1991
Highly Cited
1991
The x-ray crystal structure of a peptide corresponding to the leucine zipper of the yeast transcriptional activator GCN4 has been… Expand
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Highly Cited
1953
Highly Cited
1953
It is shown in this paper by Crick that when -helices of the same sense pack together they will probably do so about 20° away… Expand
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