Short inverse complementary amino acid sequences generate protein complexity
Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among protein registered in Swiss Prot. The observed number of princoms occurrences excee...
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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_16310691_v326_n3_p339_Goldstein |
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todo:paper_16310691_v326_n3_p339_Goldstein2023-10-03T16:28:33Z Short inverse complementary amino acid sequences generate protein complexity Goldstein, D.J. Fondrat, C. Muri, F. Nuel, G. Saragueta, P. Tocquet, A.-S. Prum, B. Genomic complexity Genomic inversions Inverse complementary amino acid disulfide DNA messenger RNA amino acid genome protein amino acid sequence article biochemistry controlled study disulfide bond gene sequence gene structure protein analysis protein function protein motif sequence database SWISS-PROT Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among protein registered in Swiss Prot. The observed number of princoms occurrences exceeds by far the expected number (p < 10-10). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes. © 2003 Académie des sciences/Éditions scientifiques et médicales Elsevier SAS. All rights reserved. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_16310691_v326_n3_p339_Goldstein |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Genomic complexity Genomic inversions Inverse complementary amino acid disulfide DNA messenger RNA amino acid genome protein amino acid sequence article biochemistry controlled study disulfide bond gene sequence gene structure protein analysis protein function protein motif sequence database SWISS-PROT |
| spellingShingle |
Genomic complexity Genomic inversions Inverse complementary amino acid disulfide DNA messenger RNA amino acid genome protein amino acid sequence article biochemistry controlled study disulfide bond gene sequence gene structure protein analysis protein function protein motif sequence database SWISS-PROT Goldstein, D.J. Fondrat, C. Muri, F. Nuel, G. Saragueta, P. Tocquet, A.-S. Prum, B. Short inverse complementary amino acid sequences generate protein complexity |
| topic_facet |
Genomic complexity Genomic inversions Inverse complementary amino acid disulfide DNA messenger RNA amino acid genome protein amino acid sequence article biochemistry controlled study disulfide bond gene sequence gene structure protein analysis protein function protein motif sequence database SWISS-PROT |
| description |
Inversions of short genomic sequences play a central role in the generation of protein complexity. More than half of the 1300 motifs registered in ProSite have protein inverse complementary sequences (princoms) among protein registered in Swiss Prot. The observed number of princoms occurrences exceeds by far the expected number (p < 10-10). Princoms often endow their host proteins with a whole new range of biochemical and physiological capabilities, including the possibility of intramolecular and intermolecular disulfide bond formation. These results support the idea that, like the duplications, the inversions of small genomic fragments have been a fundamental mechanism for shaping genomes. © 2003 Académie des sciences/Éditions scientifiques et médicales Elsevier SAS. All rights reserved. |
| format |
JOUR |
| author |
Goldstein, D.J. Fondrat, C. Muri, F. Nuel, G. Saragueta, P. Tocquet, A.-S. Prum, B. |
| author_facet |
Goldstein, D.J. Fondrat, C. Muri, F. Nuel, G. Saragueta, P. Tocquet, A.-S. Prum, B. |
| author_sort |
Goldstein, D.J. |
| title |
Short inverse complementary amino acid sequences generate protein complexity |
| title_short |
Short inverse complementary amino acid sequences generate protein complexity |
| title_full |
Short inverse complementary amino acid sequences generate protein complexity |
| title_fullStr |
Short inverse complementary amino acid sequences generate protein complexity |
| title_full_unstemmed |
Short inverse complementary amino acid sequences generate protein complexity |
| title_sort |
short inverse complementary amino acid sequences generate protein complexity |
| url |
http://hdl.handle.net/20.500.12110/paper_16310691_v326_n3_p339_Goldstein |
| work_keys_str_mv |
AT goldsteindj shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity AT fondratc shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity AT murif shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity AT nuelg shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity AT saraguetap shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity AT tocquetas shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity AT prumb shortinversecomplementaryaminoacidsequencesgenerateproteincomplexity |
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