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However, this assumption is challenged by the fact that many macromolecular complexes behave in a dynamic equilibrium with continuous conformational changes.
In practice, for many macromolecular complexes that exhibit heterogeneity with dynamic conformations and thereby an infinite conformational states, the above classification methods may not produce a good result.
As single particle cryo-electron microscopy has evolved to a new era of atomic resolution, sample heterogeneity still imposes a major limit to the resolution of many macromolecular complexes, especially those with continuous conformational flexibility.
While these methods have been proved to be very successful on the structural studies of many macromolecular complexes and revealed important mechanistic insight to the conformational switch of important molecular machines, there are still a lot of complexes with more complicated conformational heterogeneity that cannot be easily studied.
This technique, however, exposes the specimen to high ionic strength, which can cause the dissociation of many macromolecular complexes.
High-resolution cryoEM can thus provide information about protein dynamics, which is key to understanding the functions of many macromolecular complexes.
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Chromosomal DNA replication is strictly regulated through a sequence of steps that involve many macromolecular protein complexes.
Recently, two large-scale proteomics initiatives identified many novel macromolecular complexes in yeast consisting of up to several dozens of components [ 9, 10].
For many large macromolecular complexes, it has been shown that the displacements required for a system to undergo a transition between states can be described by a few normal modes.
Important classes of macromolecules, such as membrane proteins (including many receptors) and macromolecular complexes, are difficult to obtain in quantity and to crystallise, which has hampered analysis by MX.
The cytoplasm contained many discrete large macromolecular complexes, which were presumably mostly ribosomes.
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