In-cell structural biology by NMR: the benefits of the atomic scale

FX Theillet - Chemical reviews, 2022 - ACS Publications
In-cell structural biology aims at extracting structural information about proteins or nucleic
acids in their native, cellular environment. This emerging field holds great promise and is …

Mass spectrometry-based protein footprinting for higher-order structure analysis: fundamentals and applications

XR Liu, MM Zhang, ML Gross - Chemical reviews, 2020 - ACS Publications
Proteins adopt different higher-order structures (HOS) to enable their unique biological
functions. Understanding the complexities of protein higher-order structures and dynamics …

Radio signals from live cells: the coming of age of in-cell solution NMR

E Luchinat, M Cremonini, L Banci - Chemical reviews, 2022 - ACS Publications
A detailed knowledge of the complex processes that make cells and organisms alive is
fundamental in order to understand diseases and to develop novel drugs and therapeutic …

NMR-based methods for protein analysis

Y Hu, K Cheng, L He, X Zhang, B Jiang… - Analytical …, 2021 - ACS Publications
Nuclear magnetic resonance (NMR) spectroscopy is a well-established method for
analyzing protein structure, interaction, and dynamics at atomic resolution and in various …

Advanced techniques for detecting protein misfolding and aggregation in cellular environments

Y Bai, S Zhang, H Dong, Y Liu, C Liu… - Chemical Reviews, 2023 - ACS Publications
Protein misfolding and aggregation, a key contributor to the progression of numerous
neurodegenerative diseases, results in functional deficiencies and the creation of harmful …

[HTML][HTML] Biomolecular interactions modulate macromolecular structure and dynamics in atomistic model of a bacterial cytoplasm

I Yu, T Mori, T Ando, R Harada, J Jung, Y Sugita… - Elife, 2016 - elifesciences.org
Biological macromolecules function in highly crowded cellular environments. The structure
and dynamics of proteins and nucleic acids are well characterized in vitro, but in vivo …

On the binding affinity of macromolecular interactions: daring to ask why proteins interact

PL Kastritis, AMJJ Bonvin - Journal of The Royal Society …, 2013 - royalsocietypublishing.org
Interactions between proteins are orchestrated in a precise and time-dependent manner,
underlying cellular function. The binding affinity, defined as the strength of these …

Protein folding and modification in the mammalian endoplasmic reticulum

I Braakman, NJ Bulleid - Annual review of biochemistry, 2011 - annualreviews.org
Analysis of the human genome reveals that approximately a third of all open reading frames
code for proteins that enter the endoplasmic reticulum (ER), demonstrating the importance of …

Measuring protein structural changes on a proteome-wide scale using limited proteolysis-coupled mass spectrometry

S Schopper, A Kahraman, P Leuenberger, Y Feng… - Nature protocols, 2017 - nature.com
Protein structural changes induced by external perturbations or internal cues can profoundly
influence protein activity and thus modulate cellular physiology. A number of biophysical …

Global analysis of protein structural changes in complex proteomes

Y Feng, G De Franceschi, A Kahraman, M Soste… - Nature …, 2014 - nature.com
Abstract Changes in protein conformation can affect protein function, but methods to probe
these structural changes on a global scale in cells have been lacking. To enable large-scale …