Comparing proteins by their internal dynamics: Exploring structure–function relationships beyond static structural alignments
The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dy...
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Published in | Physics of life reviews Vol. 10; no. 1; pp. 1 - 26 |
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Format | Journal Article |
Language | English |
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Elsevier B.V
01.03.2013
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Abstract | The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dynamics that are functionally oriented should be subject to evolutionary conservation. Accordingly, dynamics-based protein comparisons or alignments could be used to detect protein relationships that are more elusive to sequence and structural alignments. Here we provide an account of the progress that has been made in recent years towards developing and applying general methods for comparing proteins in terms of their internal dynamics and advance the understanding of the structure–function relationship. |
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AbstractList | The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dynamics that are functionally oriented should be subject to evolutionary conservation. Accordingly, dynamics-based protein comparisons or alignments could be used to detect protein relationships that are more elusive to sequence and structural alignments. Here we provide an account of the progress that has been made in recent years towards developing and applying general methods for comparing proteins in terms of their internal dynamics and advance the understanding of the structure-function relationship. The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dynamics that are functionally oriented should be subject to evolutionary conservation. Accordingly, dynamics-based protein comparisons or alignments could be used to detect protein relationships that are more elusive to sequence and structural alignments. Here we provide an account of the progress that has been made in recent years towards developing and applying general methods for comparing proteins in terms of their internal dynamics and advance the understanding of the structure-function relationship.The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural fluctuations and conformational changes. Analogously to the case of functional structural elements, those aspects of protein flexibility and dynamics that are functionally oriented should be subject to evolutionary conservation. Accordingly, dynamics-based protein comparisons or alignments could be used to detect protein relationships that are more elusive to sequence and structural alignments. Here we provide an account of the progress that has been made in recent years towards developing and applying general methods for comparing proteins in terms of their internal dynamics and advance the understanding of the structure-function relationship. |
Author | Micheletti, Cristian |
Author_xml | – sequence: 1 givenname: Cristian surname: Micheletti fullname: Micheletti, Cristian email: michelet@sissa.it organization: Scuola Internazionale Superiore di Studi Avanzati, via Bonomea 265, Trieste, Italy |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/23199577$$D View this record in MEDLINE/PubMed |
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SubjectTerms | Animals Databases, Protein Humans Molecular Dynamics Simulation PDZ Domains Peptide Hydrolases - chemistry Peptide Hydrolases - metabolism Proteins - chemistry Proteins - metabolism Structural Homology, Protein Structure-Activity Relationship |
Title | Comparing proteins by their internal dynamics: Exploring structure–function relationships beyond static structural alignments |
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