Protein Structure Determination in Living Cells


Date

2019-05-17

Publication Type

Journal Article

ETH Bibliography

yes

Citations

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Data

Abstract

To date, in-cell NMR has elucidated various aspects of protein behaviour by associating structures in physiological conditions. Meanwhile, current studies of this method mostly have deduced protein states in cells exclusively based on ‘indirect’ structural information from peak patterns and chemical shift changes but not ‘direct’ data explicitly including interatomic distances and angles. To fully understand the functions and physical properties of proteins inside cells, it is indispensable to obtain explicit structural data or determine three-dimensional (3D) structures of proteins in cells. Whilst the short lifetime of cells in a sample tube, low sample concentrations, and massive background signals make it difficult to observe NMR signals from proteins inside cells, several methodological advances help to overcome the problems. Paramagnetic effects have an outstanding potential for in-cell structural analysis. The combination of a limited amount of experimental in-cell data with software for ab initio protein structure prediction opens an avenue to visualise 3D protein structures inside cells. Conventional nuclear Overhauser effect spectroscopy (NOESY)-based structure determination is advantageous to elucidate the conformations of side-chain atoms of proteins as well as global structures. In this article, we review current progress for the structure analysis of proteins in living systems and discuss the feasibility of its future works.

Publication status

published

Editor

Book title

Volume

20 (10)

Pages / Article No.

2442

Publisher

MDPI

Event

Edition / version

Methods

Software

Geographic location

Date collected

Date created

Subject

protein structure determination 1; non-uniform sampling 2; spectrum reconstruction 3; structural calculation 4; paramagnetic effects

Organisational unit

03782 - Riek, Roland / Riek, Roland check_circle

Notes

Funding

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