Conformational entropy in molecular recognition of intrinsically disordered proteins

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Conformational entropy in molecular recognition of intrinsically disordered proteins. / Skriver, Karen; Theisen, Frederik Friis; Kragelund, Birthe B.

I: Current Opinion in Structural Biology, Bind 83, 102697, 2023.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Skriver, K, Theisen, FF & Kragelund, BB 2023, 'Conformational entropy in molecular recognition of intrinsically disordered proteins', Current Opinion in Structural Biology, bind 83, 102697. https://doi.org/10.1016/j.sbi.2023.102697

APA

Skriver, K., Theisen, F. F., & Kragelund, B. B. (2023). Conformational entropy in molecular recognition of intrinsically disordered proteins. Current Opinion in Structural Biology, 83, [102697]. https://doi.org/10.1016/j.sbi.2023.102697

Vancouver

Skriver K, Theisen FF, Kragelund BB. Conformational entropy in molecular recognition of intrinsically disordered proteins. Current Opinion in Structural Biology. 2023;83. 102697. https://doi.org/10.1016/j.sbi.2023.102697

Author

Skriver, Karen ; Theisen, Frederik Friis ; Kragelund, Birthe B. / Conformational entropy in molecular recognition of intrinsically disordered proteins. I: Current Opinion in Structural Biology. 2023 ; Bind 83.

Bibtex

@article{79adb04a088c498f867dda39aadb4fb4,
title = "Conformational entropy in molecular recognition of intrinsically disordered proteins",
abstract = "Broad conformational ensembles make intrinsically disordered proteins or regions entropically intriguing. Although methodologically challenging and understudied, emerging studies into their changes in conformational entropy (ΔS°conf) upon complex formation have provided both quantitative and qualitative insight. Recent work based on thermodynamics from isothermal titration calorimetry and NMR spectroscopy uncovers an expanded repertoire of regulatory mechanisms, where ΔS°conf plays roles in partner selection, state behavior, functional buffering, allosteric regulation, and drug design. We highlight these mechanisms to display the large entropic reservoir of IDPs for the regulation of molecular communication. We call upon the field to make efforts to contribute to this insight as more studies are needed for forwarding mechanistic decoding of intrinsically disordered proteins and their complexes.",
keywords = "Enthalpy, IDPs, ITC, Mechanism, NMR, PPI, Thermodynamics",
author = "Karen Skriver and Theisen, {Frederik Friis} and Kragelund, {Birthe B.}",
note = "Publisher Copyright: {\textcopyright} 2023 The Author(s)",
year = "2023",
doi = "10.1016/j.sbi.2023.102697",
language = "English",
volume = "83",
journal = "Current Opinion in Structural Biology",
issn = "0959-440X",
publisher = "Elsevier Ltd. * Current Opinion Journals",

}

RIS

TY - JOUR

T1 - Conformational entropy in molecular recognition of intrinsically disordered proteins

AU - Skriver, Karen

AU - Theisen, Frederik Friis

AU - Kragelund, Birthe B.

N1 - Publisher Copyright: © 2023 The Author(s)

PY - 2023

Y1 - 2023

N2 - Broad conformational ensembles make intrinsically disordered proteins or regions entropically intriguing. Although methodologically challenging and understudied, emerging studies into their changes in conformational entropy (ΔS°conf) upon complex formation have provided both quantitative and qualitative insight. Recent work based on thermodynamics from isothermal titration calorimetry and NMR spectroscopy uncovers an expanded repertoire of regulatory mechanisms, where ΔS°conf plays roles in partner selection, state behavior, functional buffering, allosteric regulation, and drug design. We highlight these mechanisms to display the large entropic reservoir of IDPs for the regulation of molecular communication. We call upon the field to make efforts to contribute to this insight as more studies are needed for forwarding mechanistic decoding of intrinsically disordered proteins and their complexes.

AB - Broad conformational ensembles make intrinsically disordered proteins or regions entropically intriguing. Although methodologically challenging and understudied, emerging studies into their changes in conformational entropy (ΔS°conf) upon complex formation have provided both quantitative and qualitative insight. Recent work based on thermodynamics from isothermal titration calorimetry and NMR spectroscopy uncovers an expanded repertoire of regulatory mechanisms, where ΔS°conf plays roles in partner selection, state behavior, functional buffering, allosteric regulation, and drug design. We highlight these mechanisms to display the large entropic reservoir of IDPs for the regulation of molecular communication. We call upon the field to make efforts to contribute to this insight as more studies are needed for forwarding mechanistic decoding of intrinsically disordered proteins and their complexes.

KW - Enthalpy

KW - IDPs

KW - ITC

KW - Mechanism

KW - NMR

KW - PPI

KW - Thermodynamics

U2 - 10.1016/j.sbi.2023.102697

DO - 10.1016/j.sbi.2023.102697

M3 - Review

C2 - 37716093

AN - SCOPUS:85171192917

VL - 83

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

SN - 0959-440X

M1 - 102697

ER -

ID: 367900130