Frustration, function and folding
Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great...
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2018
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0959440X_v48_n_p68_Ferreiro http://hdl.handle.net/20.500.12110/paper_0959440X_v48_n_p68_Ferreiro |
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paper:paper_0959440X_v48_n_p68_Ferreiro2023-06-08T15:56:57Z Frustration, function and folding I kappa B immunoglobulin enhancer binding protein polypeptide amino acid protein protein binding amino acid sequence catalysis human priority journal protein binding protein conformation protein folding protein function protein interaction protein localization protein stability protein structure Review animal biocatalysis chemistry kinetics molecular dynamics molecular evolution physiology protein folding structure activity relation thermodynamics Amino Acid Sequence Amino Acids Animals Biocatalysis Evolution, Molecular Humans Kinetics Molecular Dynamics Simulation Protein Binding Protein Folding Proteins Structure-Activity Relationship Thermodynamics Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information. © 2017 Elsevier Ltd 2018 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0959440X_v48_n_p68_Ferreiro http://hdl.handle.net/20.500.12110/paper_0959440X_v48_n_p68_Ferreiro |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
I kappa B immunoglobulin enhancer binding protein polypeptide amino acid protein protein binding amino acid sequence catalysis human priority journal protein binding protein conformation protein folding protein function protein interaction protein localization protein stability protein structure Review animal biocatalysis chemistry kinetics molecular dynamics molecular evolution physiology protein folding structure activity relation thermodynamics Amino Acid Sequence Amino Acids Animals Biocatalysis Evolution, Molecular Humans Kinetics Molecular Dynamics Simulation Protein Binding Protein Folding Proteins Structure-Activity Relationship Thermodynamics |
| spellingShingle |
I kappa B immunoglobulin enhancer binding protein polypeptide amino acid protein protein binding amino acid sequence catalysis human priority journal protein binding protein conformation protein folding protein function protein interaction protein localization protein stability protein structure Review animal biocatalysis chemistry kinetics molecular dynamics molecular evolution physiology protein folding structure activity relation thermodynamics Amino Acid Sequence Amino Acids Animals Biocatalysis Evolution, Molecular Humans Kinetics Molecular Dynamics Simulation Protein Binding Protein Folding Proteins Structure-Activity Relationship Thermodynamics Frustration, function and folding |
| topic_facet |
I kappa B immunoglobulin enhancer binding protein polypeptide amino acid protein protein binding amino acid sequence catalysis human priority journal protein binding protein conformation protein folding protein function protein interaction protein localization protein stability protein structure Review animal biocatalysis chemistry kinetics molecular dynamics molecular evolution physiology protein folding structure activity relation thermodynamics Amino Acid Sequence Amino Acids Animals Biocatalysis Evolution, Molecular Humans Kinetics Molecular Dynamics Simulation Protein Binding Protein Folding Proteins Structure-Activity Relationship Thermodynamics |
| description |
Natural protein molecules are exceptional polymers. Encoded in apparently random strings of amino-acids, these objects perform clear physical tasks that are rare to find by simple chance. Accurate folding, specific binding, powerful catalysis, are examples of basic chemical activities that the great majority of polypeptides do not display, and are thought to be the outcome of the natural history of proteins. Function, a concept genuine to Biology, is at the core of evolution and often conflicts with the physical constraints. Locating the frustration between discrepant goals in a recurrent system leads to fundamental insights about the chances and necessities that shape the encoding of biological information. © 2017 Elsevier Ltd |
| title |
Frustration, function and folding |
| title_short |
Frustration, function and folding |
| title_full |
Frustration, function and folding |
| title_fullStr |
Frustration, function and folding |
| title_full_unstemmed |
Frustration, function and folding |
| title_sort |
frustration, function and folding |
| publishDate |
2018 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0959440X_v48_n_p68_Ferreiro http://hdl.handle.net/20.500.12110/paper_0959440X_v48_n_p68_Ferreiro |
| _version_ |
1768545519127232512 |