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 inPhysics of life reviews Vol. 10; no. 1; pp. 1 - 26
Main Author Micheletti, Cristian
Format Journal Article
LanguageEnglish
Published Netherlands 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.
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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Snippet The growing interest for comparing protein internal dynamics owes much to the realisation that protein function can be accompanied or assisted by structural...
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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
URI https://dx.doi.org/10.1016/j.plrev.2012.10.009
https://www.ncbi.nlm.nih.gov/pubmed/23199577
https://www.proquest.com/docview/1328229076
Volume 10
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