Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Standard

Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets. / Sagar, Amin; Herranz-Trillo, Fátima; Langkilde, Annette Eva; Vestergaard, Bente; Bernadó, Pau.

I: Structure, Bind 29, Nr. 9, 2021, s. 1074-1090.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sagar, A, Herranz-Trillo, F, Langkilde, AE, Vestergaard, B & Bernadó, P 2021, 'Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets', Structure, bind 29, nr. 9, s. 1074-1090. https://doi.org/10.1016/j.str.2021.03.017

APA

Sagar, A., Herranz-Trillo, F., Langkilde, A. E., Vestergaard, B., & Bernadó, P. (2021). Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets. Structure, 29(9), 1074-1090. https://doi.org/10.1016/j.str.2021.03.017

Vancouver

Sagar A, Herranz-Trillo F, Langkilde AE, Vestergaard B, Bernadó P. Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets. Structure. 2021;29(9):1074-1090. https://doi.org/10.1016/j.str.2021.03.017

Author

Sagar, Amin ; Herranz-Trillo, Fátima ; Langkilde, Annette Eva ; Vestergaard, Bente ; Bernadó, Pau. / Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets. I: Structure. 2021 ; Bind 29, Nr. 9. s. 1074-1090.

Bibtex

@article{9f5865d337a648b4b265a7f20c3ef909,
title = "Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets",
abstract = "Transient biomolecular interactions play crucial roles in many cellular signaling and regulation processes. However, deciphering the structure of these assemblies is challenging owing to the difficulties in isolating complexes from the individual partners. The additive nature of small-angle X-ray scattering (SAXS) data allows for probing the species present in these mixtures, but decomposition into structural and thermodynamic information is difficult. We present a chemometric approach enabling the decomposition of titration SAXS data into species-specific information. Using extensive synthetic SAXS data, we demonstrate that robust decomposition can be achieved for titrations with a maximum fraction of complex of 0.5 that can be extended to 0.3 when two orthogonal titrations are simultaneously analyzed. The effect of the structural features, titration points, relative concentrations, and noise are thoroughly analyzed. The validation of the strategy with experimental data highlights the power of the approach to provide unique insights into this family of biomolecular assemblies.",
author = "Amin Sagar and F{\'a}tima Herranz-Trillo and Langkilde, {Annette Eva} and Bente Vestergaard and Pau Bernad{\'o}",
note = "Copyright {\textcopyright} 2021 Elsevier Ltd. All rights reserved.",
year = "2021",
doi = "10.1016/j.str.2021.03.017",
language = "English",
volume = "29",
pages = "1074--1090",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "9",

}

RIS

TY - JOUR

T1 - Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets

AU - Sagar, Amin

AU - Herranz-Trillo, Fátima

AU - Langkilde, Annette Eva

AU - Vestergaard, Bente

AU - Bernadó, Pau

N1 - Copyright © 2021 Elsevier Ltd. All rights reserved.

PY - 2021

Y1 - 2021

N2 - Transient biomolecular interactions play crucial roles in many cellular signaling and regulation processes. However, deciphering the structure of these assemblies is challenging owing to the difficulties in isolating complexes from the individual partners. The additive nature of small-angle X-ray scattering (SAXS) data allows for probing the species present in these mixtures, but decomposition into structural and thermodynamic information is difficult. We present a chemometric approach enabling the decomposition of titration SAXS data into species-specific information. Using extensive synthetic SAXS data, we demonstrate that robust decomposition can be achieved for titrations with a maximum fraction of complex of 0.5 that can be extended to 0.3 when two orthogonal titrations are simultaneously analyzed. The effect of the structural features, titration points, relative concentrations, and noise are thoroughly analyzed. The validation of the strategy with experimental data highlights the power of the approach to provide unique insights into this family of biomolecular assemblies.

AB - Transient biomolecular interactions play crucial roles in many cellular signaling and regulation processes. However, deciphering the structure of these assemblies is challenging owing to the difficulties in isolating complexes from the individual partners. The additive nature of small-angle X-ray scattering (SAXS) data allows for probing the species present in these mixtures, but decomposition into structural and thermodynamic information is difficult. We present a chemometric approach enabling the decomposition of titration SAXS data into species-specific information. Using extensive synthetic SAXS data, we demonstrate that robust decomposition can be achieved for titrations with a maximum fraction of complex of 0.5 that can be extended to 0.3 when two orthogonal titrations are simultaneously analyzed. The effect of the structural features, titration points, relative concentrations, and noise are thoroughly analyzed. The validation of the strategy with experimental data highlights the power of the approach to provide unique insights into this family of biomolecular assemblies.

U2 - 10.1016/j.str.2021.03.017

DO - 10.1016/j.str.2021.03.017

M3 - Journal article

C2 - 33862013

VL - 29

SP - 1074

EP - 1090

JO - Structure

JF - Structure

SN - 0969-2126

IS - 9

ER -

ID: 260200082