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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Autores principales: Parra, R.G., Espada, R., Verstraete, N., Ferreiro, D.U.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_1553734X_v11_n12_p_Parra
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spelling 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
collection 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
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AT verstraeten structuralandenergeticcharacterizationoftheankyrinrepeatproteinfamily
AT ferreirodu structuralandenergeticcharacterizationoftheankyrinrepeatproteinfamily
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