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- Andrei Lupas
- Department of Molecular Biology, Princeton University, Princeton, NJ 08544
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- Marc Van Dyke
- Department of Molecular Biology, Princeton University, Princeton, NJ 08544
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- Jeff Stock
- Department of Molecular Biology, Princeton University, Princeton, NJ 08544
説明
<jats:p>The probability that a residue in a protein is part of a coiled-coil structure was assessed by comparison of its flanking sequences with sequences of known coiled-coil proteins. This method was used to delineate coiled-coil domains in otherwise globular proteins, such as the leucine zipper domains in transcriptional regulators, and to predict regions of discontinuity within coiled-coil structures, such as the hinge region in myosin. More than 200 proteins that probably have coiled-coil domains were identified in GenBank, including α- and β-tubulins, flagellins, G protein β subunits, some bacterial transfer RNA synthetases, and members of the heat shock protein (Hsp70) family.</jats:p>
収録刊行物
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- Science
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Science 252 (5009), 1162-1164, 1991-05-24
American Association for the Advancement of Science (AAAS)
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詳細情報 詳細情報について
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- CRID
- 1360011144939510400
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- NII論文ID
- 80005924648
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- ISSN
- 10959203
- 00368075
- http://id.crossref.org/issn/00368075
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- データソース種別
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- Crossref
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