Functional aspects of protein flexibility

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Standard

Functional aspects of protein flexibility. / Teilum, Kaare; Olsen, Johan G; Kragelund, Birthe B.

I: Cellular and Molecular Life Sciences, Bind 66, Nr. 14, 2009, s. 2231-47.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Teilum, K, Olsen, JG & Kragelund, BB 2009, 'Functional aspects of protein flexibility', Cellular and Molecular Life Sciences, bind 66, nr. 14, s. 2231-47. https://doi.org/10.1007/s00018-009-0014-6

APA

Teilum, K., Olsen, J. G., & Kragelund, B. B. (2009). Functional aspects of protein flexibility. Cellular and Molecular Life Sciences, 66(14), 2231-47. https://doi.org/10.1007/s00018-009-0014-6

Vancouver

Teilum K, Olsen JG, Kragelund BB. Functional aspects of protein flexibility. Cellular and Molecular Life Sciences. 2009;66(14):2231-47. https://doi.org/10.1007/s00018-009-0014-6

Author

Teilum, Kaare ; Olsen, Johan G ; Kragelund, Birthe B. / Functional aspects of protein flexibility. I: Cellular and Molecular Life Sciences. 2009 ; Bind 66, Nr. 14. s. 2231-47.

Bibtex

@article{2fa124d0bd6511debda0000ea68e967b,
title = "Functional aspects of protein flexibility",
abstract = "Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among cells and even between organisms. Appreciation of the non-static nature of proteins is emerging, but to describe and incorporate this into an intuitive perception of protein function is challenging. Flexibility is of overwhelming importance for protein function, and the changes in protein structure during interactions with binding partners can be dramatic. The present review addresses protein flexibility, focusing on protein-ligand interactions. The thermodynamics involved are reviewed, and examples of structure-function studies involving experimentally determined flexibility descriptions are presented. While much remains to be understood about protein flexibility, it is clear that it is encoded within their amino acid sequence and should be viewed as an integral part of their structure.",
author = "Kaare Teilum and Olsen, {Johan G} and Kragelund, {Birthe B}",
note = "Keywords: Binding Sites; Ligands; Models, Molecular; Protein Binding; Protein Conformation; Proteins; Structure-Activity Relationship; Thermodynamics",
year = "2009",
doi = "10.1007/s00018-009-0014-6",
language = "English",
volume = "66",
pages = "2231--47",
journal = "EXS",
issn = "1023-294X",
publisher = "Springer Basel AG",
number = "14",

}

RIS

TY - JOUR

T1 - Functional aspects of protein flexibility

AU - Teilum, Kaare

AU - Olsen, Johan G

AU - Kragelund, Birthe B

N1 - Keywords: Binding Sites; Ligands; Models, Molecular; Protein Binding; Protein Conformation; Proteins; Structure-Activity Relationship; Thermodynamics

PY - 2009

Y1 - 2009

N2 - Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among cells and even between organisms. Appreciation of the non-static nature of proteins is emerging, but to describe and incorporate this into an intuitive perception of protein function is challenging. Flexibility is of overwhelming importance for protein function, and the changes in protein structure during interactions with binding partners can be dramatic. The present review addresses protein flexibility, focusing on protein-ligand interactions. The thermodynamics involved are reviewed, and examples of structure-function studies involving experimentally determined flexibility descriptions are presented. While much remains to be understood about protein flexibility, it is clear that it is encoded within their amino acid sequence and should be viewed as an integral part of their structure.

AB - Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among cells and even between organisms. Appreciation of the non-static nature of proteins is emerging, but to describe and incorporate this into an intuitive perception of protein function is challenging. Flexibility is of overwhelming importance for protein function, and the changes in protein structure during interactions with binding partners can be dramatic. The present review addresses protein flexibility, focusing on protein-ligand interactions. The thermodynamics involved are reviewed, and examples of structure-function studies involving experimentally determined flexibility descriptions are presented. While much remains to be understood about protein flexibility, it is clear that it is encoded within their amino acid sequence and should be viewed as an integral part of their structure.

U2 - 10.1007/s00018-009-0014-6

DO - 10.1007/s00018-009-0014-6

M3 - Journal article

C2 - 19308324

VL - 66

SP - 2231

EP - 2247

JO - EXS

JF - EXS

SN - 1023-294X

IS - 14

ER -

ID: 15288486