author_facet Liu, Yang
Gerstein, Mark
Engelman, Donald M.
Liu, Yang
Gerstein, Mark
Engelman, Donald M.
author Liu, Yang
Gerstein, Mark
Engelman, Donald M.
spellingShingle Liu, Yang
Gerstein, Mark
Engelman, Donald M.
Proceedings of the National Academy of Sciences
Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
Multidisciplinary
author_sort liu, yang
spelling Liu, Yang Gerstein, Mark Engelman, Donald M. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0307330101 <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p> Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism Proceedings of the National Academy of Sciences
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title Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_unstemmed Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_full Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_fullStr Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_full_unstemmed Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_short Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_sort transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.0307330101
publishDate 2004
physical 3495-3497
description <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p>
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author Liu, Yang, Gerstein, Mark, Engelman, Donald M.
author_facet Liu, Yang, Gerstein, Mark, Engelman, Donald M., Liu, Yang, Gerstein, Mark, Engelman, Donald M.
author_sort liu, yang
container_issue 10
container_start_page 3495
container_title Proceedings of the National Academy of Sciences
container_volume 101
description <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p>
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imprint Proceedings of the National Academy of Sciences, 2004
imprint_str_mv Proceedings of the National Academy of Sciences, 2004
institution DE-Pl11, DE-Rs1, DE-14, DE-105, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Zi4, DE-Gla1, DE-15
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spelling Liu, Yang Gerstein, Mark Engelman, Donald M. 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.0307330101 <jats:p>Recombination of evolutionarily unrelated domains is a mechanism often used by evolution to produce variety in soluble proteins. By using a classification of polytopic transmembrane domains into families, we examined integral membrane proteins for evidence of this mechanism. Surprisingly, we found that domain recombination is not common for the transmembrane regions of membrane proteins, a majority of integral membrane proteins containing only a single transmembrane domain. We suggest that noncovalent oligomeric associations, which are common in membrane proteins, may provide an alternative source of evolutionary diversity.</jats:p> Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism Proceedings of the National Academy of Sciences
spellingShingle Liu, Yang, Gerstein, Mark, Engelman, Donald M., Proceedings of the National Academy of Sciences, Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism, Multidisciplinary
title Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_full Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_fullStr Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_full_unstemmed Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_short Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_sort transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
title_unstemmed Transmembrane protein domains rarely use covalent domain recombination as an evolutionary mechanism
topic Multidisciplinary
url http://dx.doi.org/10.1073/pnas.0307330101