Protein fibrillation from another small angle—SAXS data analysis of developing systems

Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt

Standard

Protein fibrillation from another small angle—SAXS data analysis of developing systems. / Langkilde, Annette Eva; Vestergaard, Bente.

Methods in Enzymology. Bind 678 Elsevier, 2023. s. 377-409.

Publikation: Bidrag til bog/antologi/rapport › Bidrag til bog/antologi › Forskning › fagfællebedømt

Harvard

Langkilde, AE & Vestergaard, B 2023, Protein fibrillation from another small angle—SAXS data analysis of developing systems. i Methods in Enzymology. bind 678, Elsevier, s. 377-409. https://doi.org/10.1016/bs.mie.2022.09.025

APA

Langkilde, A. E., & Vestergaard, B. (2023). Protein fibrillation from another small angle—SAXS data analysis of developing systems. I Methods in Enzymology (Bind 678, s. 377-409). Elsevier. https://doi.org/10.1016/bs.mie.2022.09.025

Vancouver

Langkilde AE, Vestergaard B. Protein fibrillation from another small angle—SAXS data analysis of developing systems. I Methods in Enzymology. Bind 678. Elsevier. 2023. s. 377-409 https://doi.org/10.1016/bs.mie.2022.09.025

Author

Langkilde, Annette Eva ; Vestergaard, Bente. / Protein fibrillation from another small angle—SAXS data analysis of developing systems. Methods in Enzymology. Bind 678 Elsevier, 2023. s. 377-409

Bibtex

@inbook{9aa71692bec64f368d95fb01cb19435f,
title = "Protein fibrillation from another small angle—SAXS data analysis of developing systems",
abstract = "During the fibrillation process amyloid proteins undergo structural changes at very different length and time scales. Small angle X-ray scattering (SAXS) is a method that is uniquely suitable for the structural analysis of this process. Careful measures must, however, be taken both in the sample preparation, data collection and data analysis procedures to ensure proper data quality, coverage of the process and reliable interpretation. With this chapter, we provide many details about the data analysis of such developing systems. The recommendations are based on our own experience with analysis of data from several amyloid and amyloid-like proteins, with data decomposition being a central point in the procedure. We focus on two alternative approaches, one being a laborious, hands-on, iterative approach, the other being more automated, applying a chemometrics based software, developed for the purpose. Both methods can equally well be applied to other developing mixtures, but specific recommendations for amyloid samples are emphasized in this chapter.",
author = "Langkilde, {Annette Eva} and Bente Vestergaard",
year = "2023",
doi = "10.1016/bs.mie.2022.09.025",
language = "English",
volume = "678",
pages = "377--409",
booktitle = "Methods in Enzymology",
publisher = "Elsevier",
address = "Netherlands",

}

RIS

TY - CHAP

T1 - Protein fibrillation from another small angle—SAXS data analysis of developing systems

AU - Langkilde, Annette Eva

AU - Vestergaard, Bente

PY - 2023

Y1 - 2023

N2 - During the fibrillation process amyloid proteins undergo structural changes at very different length and time scales. Small angle X-ray scattering (SAXS) is a method that is uniquely suitable for the structural analysis of this process. Careful measures must, however, be taken both in the sample preparation, data collection and data analysis procedures to ensure proper data quality, coverage of the process and reliable interpretation. With this chapter, we provide many details about the data analysis of such developing systems. The recommendations are based on our own experience with analysis of data from several amyloid and amyloid-like proteins, with data decomposition being a central point in the procedure. We focus on two alternative approaches, one being a laborious, hands-on, iterative approach, the other being more automated, applying a chemometrics based software, developed for the purpose. Both methods can equally well be applied to other developing mixtures, but specific recommendations for amyloid samples are emphasized in this chapter.

AB - During the fibrillation process amyloid proteins undergo structural changes at very different length and time scales. Small angle X-ray scattering (SAXS) is a method that is uniquely suitable for the structural analysis of this process. Careful measures must, however, be taken both in the sample preparation, data collection and data analysis procedures to ensure proper data quality, coverage of the process and reliable interpretation. With this chapter, we provide many details about the data analysis of such developing systems. The recommendations are based on our own experience with analysis of data from several amyloid and amyloid-like proteins, with data decomposition being a central point in the procedure. We focus on two alternative approaches, one being a laborious, hands-on, iterative approach, the other being more automated, applying a chemometrics based software, developed for the purpose. Both methods can equally well be applied to other developing mixtures, but specific recommendations for amyloid samples are emphasized in this chapter.

U2 - 10.1016/bs.mie.2022.09.025

DO - 10.1016/bs.mie.2022.09.025

M3 - Book chapter

C2 - 36641215

VL - 678

SP - 377

EP - 409

BT - Methods in Enzymology

PB - Elsevier

ER -

ID: 324686155