Protein fibrillation from another small angle: Sample preparation and SAXS data collection

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

Standard

Protein fibrillation from another small angle: Sample preparation and SAXS data collection. / Vestergaard, Bente; Langkilde, Annette Eva.

Methods in Enzymology. Bind 677 Academic Press, 2022. s. 291-321 (Methods in Enzymology).

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

Harvard

Vestergaard, B & Langkilde, AE 2022, Protein fibrillation from another small angle: Sample preparation and SAXS data collection. i Methods in Enzymology. bind 677, Academic Press, Methods in Enzymology, s. 291-321. https://doi.org/10.1016/bs.mie.2022.08.041

APA

Vestergaard, B., & Langkilde, A. E. (2022). Protein fibrillation from another small angle: Sample preparation and SAXS data collection. I Methods in Enzymology (Bind 677, s. 291-321). Academic Press. Methods in Enzymology https://doi.org/10.1016/bs.mie.2022.08.041

Vancouver

Vestergaard B, Langkilde AE. Protein fibrillation from another small angle: Sample preparation and SAXS data collection. I Methods in Enzymology. Bind 677. Academic Press. 2022. s. 291-321. (Methods in Enzymology). https://doi.org/10.1016/bs.mie.2022.08.041

Author

Vestergaard, Bente ; Langkilde, Annette Eva. / Protein fibrillation from another small angle: Sample preparation and SAXS data collection. Methods in Enzymology. Bind 677 Academic Press, 2022. s. 291-321 (Methods in Enzymology).

Bibtex

@inbook{7fc8585c57934ff6a095d811b00ea650,
title = "Protein fibrillation from another small angle: Sample preparation and SAXS data collection",
abstract = "Protein fibrillation associates with several chronic, progressive, and fatal disorders, counting well-known maladies as Parkinson's, Alzheimer's, and Huntington's disease. The fibrillation process includes structural changes and aggregation of the disease specific protein, resulting in a mixture of different structural states covering nm to μm scale in varying volume fractions. SAXS uniquely enables structural investigations of such evolving mixtures but requires that the underlying main data collection experiment is carefully prepared. In this chapter, we provide very detailed instructions on how to plan and perform such protein fibrillation experiments, both before and during the SAXS data collection. The chapter is based on our own experience mainly using high-end synchrotron radiation facilities for the data collection but can equally well be applied on state-of-the-art laboratory based SAXS instruments. We accumulate the know-how from our group, established via the study of different amyloid-like proteins, applying fibrillation either in batch or in plate reader, with or without known process quenching conditions.",
author = "Bente Vestergaard and Langkilde, {Annette Eva}",
year = "2022",
doi = "10.1016/bs.mie.2022.08.041",
language = "English",
volume = "677",
series = "Methods in Enzymology",
publisher = "Academic Press",
pages = "291--321",
booktitle = "Methods in Enzymology",
address = "United States",

}

RIS

TY - CHAP

T1 - Protein fibrillation from another small angle: Sample preparation and SAXS data collection

AU - Vestergaard, Bente

AU - Langkilde, Annette Eva

PY - 2022

Y1 - 2022

N2 - Protein fibrillation associates with several chronic, progressive, and fatal disorders, counting well-known maladies as Parkinson's, Alzheimer's, and Huntington's disease. The fibrillation process includes structural changes and aggregation of the disease specific protein, resulting in a mixture of different structural states covering nm to μm scale in varying volume fractions. SAXS uniquely enables structural investigations of such evolving mixtures but requires that the underlying main data collection experiment is carefully prepared. In this chapter, we provide very detailed instructions on how to plan and perform such protein fibrillation experiments, both before and during the SAXS data collection. The chapter is based on our own experience mainly using high-end synchrotron radiation facilities for the data collection but can equally well be applied on state-of-the-art laboratory based SAXS instruments. We accumulate the know-how from our group, established via the study of different amyloid-like proteins, applying fibrillation either in batch or in plate reader, with or without known process quenching conditions.

AB - Protein fibrillation associates with several chronic, progressive, and fatal disorders, counting well-known maladies as Parkinson's, Alzheimer's, and Huntington's disease. The fibrillation process includes structural changes and aggregation of the disease specific protein, resulting in a mixture of different structural states covering nm to μm scale in varying volume fractions. SAXS uniquely enables structural investigations of such evolving mixtures but requires that the underlying main data collection experiment is carefully prepared. In this chapter, we provide very detailed instructions on how to plan and perform such protein fibrillation experiments, both before and during the SAXS data collection. The chapter is based on our own experience mainly using high-end synchrotron radiation facilities for the data collection but can equally well be applied on state-of-the-art laboratory based SAXS instruments. We accumulate the know-how from our group, established via the study of different amyloid-like proteins, applying fibrillation either in batch or in plate reader, with or without known process quenching conditions.

U2 - 10.1016/bs.mie.2022.08.041

DO - 10.1016/bs.mie.2022.08.041

M3 - Book chapter

C2 - 36410953

VL - 677

T3 - Methods in Enzymology

SP - 291

EP - 321

BT - Methods in Enzymology

PB - Academic Press

ER -

ID: 321161688