Structural and Energetic Characterization of the Ankyrin Repeat Protein Family
Ankyrin repeat containing proteins are one of the most abundant solenoid folds. Usually implicated in specific protein-protein interactions, these proteins are readily amenable for design, with promising biotechnological and biomedical applications. Studying repeat protein families presents technica...
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Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_1553734X_v11_n12_p_Parra |
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todo:paper_1553734X_v11_n12_p_Parra2023-10-03T16:25:26Z Structural and Energetic Characterization of the Ankyrin Repeat Protein Family Parra, R.G. Espada, R. Verstraete, N. Ferreiro, D.U. ankyrin amino acid sequence chemical model chemistry computer simulation energy transfer molecular genetics molecular model procedures sequence analysis ultrastructure Amino Acid Sequence Ankyrin Repeat Ankyrins Computer Simulation Energy Transfer Models, Chemical Models, Molecular Molecular Sequence Data Sequence Analysis, Protein Ankyrin repeat containing proteins are one of the most abundant solenoid folds. Usually implicated in specific protein-protein interactions, these proteins are readily amenable for design, with promising biotechnological and biomedical applications. Studying repeat protein families presents technical challenges due to the high sequence divergence among the repeating units. We developed and applied a systematic method to consistently identify and annotate the structural repetitions over the members of the complete Ankyrin Repeat Protein Family, with increased sensitivity over previous studies. We statistically characterized the number of repeats, the folding of the repeat-arrays, their structural variations, insertions and deletions. An energetic analysis of the local frustration patterns reveal the basic features underlying fold stability and its relation to the functional binding regions. We found a strong linear correlation between the conservation of the energetic features in the repeat arrays and their sequence variations, and discuss new insights into the organization and function of these ubiquitous proteins. © 2015 Parra et al. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_1553734X_v11_n12_p_Parra |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
ankyrin amino acid sequence chemical model chemistry computer simulation energy transfer molecular genetics molecular model procedures sequence analysis ultrastructure Amino Acid Sequence Ankyrin Repeat Ankyrins Computer Simulation Energy Transfer Models, Chemical Models, Molecular Molecular Sequence Data Sequence Analysis, Protein |
spellingShingle |
ankyrin amino acid sequence chemical model chemistry computer simulation energy transfer molecular genetics molecular model procedures sequence analysis ultrastructure Amino Acid Sequence Ankyrin Repeat Ankyrins Computer Simulation Energy Transfer Models, Chemical Models, Molecular Molecular Sequence Data Sequence Analysis, Protein Parra, R.G. Espada, R. Verstraete, N. Ferreiro, D.U. Structural and Energetic Characterization of the Ankyrin Repeat Protein Family |
topic_facet |
ankyrin amino acid sequence chemical model chemistry computer simulation energy transfer molecular genetics molecular model procedures sequence analysis ultrastructure Amino Acid Sequence Ankyrin Repeat Ankyrins Computer Simulation Energy Transfer Models, Chemical Models, Molecular Molecular Sequence Data Sequence Analysis, Protein |
description |
Ankyrin repeat containing proteins are one of the most abundant solenoid folds. Usually implicated in specific protein-protein interactions, these proteins are readily amenable for design, with promising biotechnological and biomedical applications. Studying repeat protein families presents technical challenges due to the high sequence divergence among the repeating units. We developed and applied a systematic method to consistently identify and annotate the structural repetitions over the members of the complete Ankyrin Repeat Protein Family, with increased sensitivity over previous studies. We statistically characterized the number of repeats, the folding of the repeat-arrays, their structural variations, insertions and deletions. An energetic analysis of the local frustration patterns reveal the basic features underlying fold stability and its relation to the functional binding regions. We found a strong linear correlation between the conservation of the energetic features in the repeat arrays and their sequence variations, and discuss new insights into the organization and function of these ubiquitous proteins. © 2015 Parra et al. |
format |
JOUR |
author |
Parra, R.G. Espada, R. Verstraete, N. Ferreiro, D.U. |
author_facet |
Parra, R.G. Espada, R. Verstraete, N. Ferreiro, D.U. |
author_sort |
Parra, R.G. |
title |
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family |
title_short |
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family |
title_full |
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family |
title_fullStr |
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family |
title_full_unstemmed |
Structural and Energetic Characterization of the Ankyrin Repeat Protein Family |
title_sort |
structural and energetic characterization of the ankyrin repeat protein family |
url |
http://hdl.handle.net/20.500.12110/paper_1553734X_v11_n12_p_Parra |
work_keys_str_mv |
AT parrarg structuralandenergeticcharacterizationoftheankyrinrepeatproteinfamily AT espadar structuralandenergeticcharacterizationoftheankyrinrepeatproteinfamily AT verstraeten structuralandenergeticcharacterizationoftheankyrinrepeatproteinfamily AT ferreirodu structuralandenergeticcharacterizationoftheankyrinrepeatproteinfamily |
_version_ |
1807317149530718208 |