Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

Membrane proteins are flexible molecular machines, responsible for the exchange of molecules in and out of the cell, which have evolved to perform specific and complex tasks with great efficiency. Obtaining accurate descriptions of their dynamics in the context of their function represents a major challenge for structural biology. Here we chart recent developments in mass spectrometry designed to characterize changes in the dynamics of membrane proteins in response to ligand binding or post-translational modifications. We focus on cooperative movements and structural changes across a range of timescales, from milliseconds to minutes, and highlight the contributions of mass spectrometry to our understanding of molecular mechanisms of diverse transmembrane processes.

Original publication




Journal article


Curr Opin Struct Biol

Publication Date





122 - 130


Ions, Mass Spectrometry, Membrane Proteins, Models, Molecular, Protein Conformation