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
APA
Vancouver
Author
Bibtex
}
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