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小角中子散射对比变化研究生物复合物:挑战与成功。

Small-angle neutron scattering contrast variation studies of biological complexes: Challenges and triumphs.

机构信息

NIST Center for Neutron Research, NIST, Gaithersburg, MD, 20899, USA.

出版信息

Curr Opin Struct Biol. 2022 Jun;74:102375. doi: 10.1016/j.sbi.2022.102375. Epub 2022 Apr 28.


DOI:10.1016/j.sbi.2022.102375
PMID:35490650
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10988784/
Abstract

Small-angle neutron scattering (SANS) has been a beneficial tool for studying the structure of biological macromolecules in solution for several decades. Continued improvements in sample preparation techniques, including deuterium labeling, neutron instrumentation and complementary techniques such as small-angle x-ray scattering (SAXS), cryo-EM, NMR and x-ray crystallography, along with the availability of more powerful structure prediction algorithms and computational resources has made SANS more important than ever as a means to obtain unique information on the structure of biological complexes in solution. In particular, the contrast variation (CV) technique, which requires a large commitment in both sample preparation and measurement time, has become more practical with the advent of these improved resources. Here, challenges and recent triumphs as well as future prospects are discussed.

摘要

小角中子散射(SANS)技术在过去几十年中一直是研究生物大分子在溶液中结构的有益工具。随着氘标记、中子仪器以及小角 X 射线散射(SAXS)、冷冻电镜、NMR 和 X 射线晶体学等互补技术的不断改进,以及更强大的结构预测算法和计算资源的可用性,SANS 作为一种获取溶液中生物复合物结构独特信息的手段变得比以往任何时候都更加重要。特别是对比变化(CV)技术,随着这些改进资源的出现,它在样品制备和测量时间方面都需要大量的投入,变得更加实用。在这里,我们将讨论这项技术所面临的挑战、最近的成功以及未来的前景。

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本文引用的文献

[1]
Reversible Self-Association in Lactate Dehydrogenase during Freeze-Thaw in Buffered Solutions Using Neutron Scattering.

Mol Pharm. 2021-12-6

[2]
Elongation rate and average length of amyloid fibrils in solution using isotope-labelled small-angle neutron scattering.

RSC Chem Biol. 2021-4-14

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Highly accurate protein structure prediction for the human proteome.

Nature. 2021-8

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Science. 2021-8-20

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Highly accurate protein structure prediction with AlphaFold.

Nature. 2021-8

[6]
Current limits of structural biology: The transient interaction between cytochrome and photosystem I.

Curr Res Struct Biol. 2020-8-26

[7]
Transient and stabilized complexes of Nsp7, Nsp8, and Nsp12 in SARS-CoV-2 replication.

Biophys J. 2021-8-3

[8]
Functionalized lipid nanoparticles for subcutaneous administration of mRNA to achieve systemic exposures of a therapeutic protein.

Mol Ther Nucleic Acids. 2021-3-13

[9]
Apolipoprotein E Binding Drives Structural and Compositional Rearrangement of mRNA-Containing Lipid Nanoparticles.

ACS Nano. 2021-4-27

[10]
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase.

J Struct Biol. 2021-6

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