Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness. / Olsen, Johan Gotthardt; Teilum, Kaare; Kragelund, Birthe Brandt.

I: Cellular and Molecular Life Sciences, Bind 74, Nr. 17, 09.2017, s. 3175-3183.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Olsen, JG, Teilum, K & Kragelund, BB 2017, 'Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness', Cellular and Molecular Life Sciences, bind 74, nr. 17, s. 3175-3183. https://doi.org/10.1007/s00018-017-2560-7

APA

Olsen, J. G., Teilum, K., & Kragelund, B. B. (2017). Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness. Cellular and Molecular Life Sciences, 74(17), 3175-3183. https://doi.org/10.1007/s00018-017-2560-7

Vancouver

Olsen JG, Teilum K, Kragelund BB. Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness. Cellular and Molecular Life Sciences. 2017 sep.;74(17):3175-3183. https://doi.org/10.1007/s00018-017-2560-7

Author

Olsen, Johan Gotthardt ; Teilum, Kaare ; Kragelund, Birthe Brandt. / Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness. I: Cellular and Molecular Life Sciences. 2017 ; Bind 74, Nr. 17. s. 3175-3183.

Bibtex

@article{89d3199202c94fa89498e88a5511ac52,
title = "Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness",
abstract = "Intrinsically disordered proteins (IDPs) do not, by themselves, fold into a compact globular structure. They are extremely dynamic and flexible, and are typically involved in signalling and transduction of information through binding to other macromolecules. The reason for their existence may lie in their malleability, which enables them to bind several different partners with high specificity. In addition, their interactions with other macromolecules can be regulated by a variable amount of chemically diverse post-translational modifications. Four kinetically and energetically different types of complexes between an IDP and another macromolecule are reviewed: (1) simple two-state binding involving a single binding site, (2) avidity, (3) allovalency and (4) fuzzy binding; the last three involving more than one site. Finally, a qualitative definition of fuzzy binding is suggested, examples are provided, and its distinction to allovalency and avidity is highlighted and discussed.",
keywords = "Journal Article, Review",
author = "Olsen, {Johan Gotthardt} and Kaare Teilum and Kragelund, {Birthe Brandt}",
year = "2017",
month = sep,
doi = "10.1007/s00018-017-2560-7",
language = "English",
volume = "74",
pages = "3175--3183",
journal = "EXS",
issn = "1023-294X",
publisher = "Springer Basel AG",
number = "17",

}

RIS

TY - JOUR

T1 - Behaviour of intrinsically disordered proteins in protein-protein complexes with an emphasis on fuzziness

AU - Olsen, Johan Gotthardt

AU - Teilum, Kaare

AU - Kragelund, Birthe Brandt

PY - 2017/9

Y1 - 2017/9

N2 - Intrinsically disordered proteins (IDPs) do not, by themselves, fold into a compact globular structure. They are extremely dynamic and flexible, and are typically involved in signalling and transduction of information through binding to other macromolecules. The reason for their existence may lie in their malleability, which enables them to bind several different partners with high specificity. In addition, their interactions with other macromolecules can be regulated by a variable amount of chemically diverse post-translational modifications. Four kinetically and energetically different types of complexes between an IDP and another macromolecule are reviewed: (1) simple two-state binding involving a single binding site, (2) avidity, (3) allovalency and (4) fuzzy binding; the last three involving more than one site. Finally, a qualitative definition of fuzzy binding is suggested, examples are provided, and its distinction to allovalency and avidity is highlighted and discussed.

AB - Intrinsically disordered proteins (IDPs) do not, by themselves, fold into a compact globular structure. They are extremely dynamic and flexible, and are typically involved in signalling and transduction of information through binding to other macromolecules. The reason for their existence may lie in their malleability, which enables them to bind several different partners with high specificity. In addition, their interactions with other macromolecules can be regulated by a variable amount of chemically diverse post-translational modifications. Four kinetically and energetically different types of complexes between an IDP and another macromolecule are reviewed: (1) simple two-state binding involving a single binding site, (2) avidity, (3) allovalency and (4) fuzzy binding; the last three involving more than one site. Finally, a qualitative definition of fuzzy binding is suggested, examples are provided, and its distinction to allovalency and avidity is highlighted and discussed.

KW - Journal Article

KW - Review

U2 - 10.1007/s00018-017-2560-7

DO - 10.1007/s00018-017-2560-7

M3 - Review

C2 - 28597296

VL - 74

SP - 3175

EP - 3183

JO - EXS

JF - EXS

SN - 1023-294X

IS - 17

ER -

ID: 180068631