Abstract:
:A synopsis of in-cell NMR spectroscopic approaches to study interaction proteomics in prokaryotic and eukaryotic cells is presented. We describe the use of in-cell NMR spectroscopy to resolve high resolution protein structures, discuss methodologies for determining and analyzing high and low affinity protein-target structural interactions, including intrinsically disordered proteins, and detail important functional interactions that result from these interactions. SIGNIFICANCE: The ultimate goal of structural and biochemical research is to understand how macromolecular interactions give rise to and regulate biological activity in living cells. The challenge is formidable due to the complexity that arises not only from the number of proteins (genes) expressed by the organism, but also from the combinatorial interactions between them. Despite ongoing efforts to decipher the complex nature of protein interactions, new methods for structurally characterizing protein complexes are needed to fully understand molecular networks. With the onset of in-cell NMR spectroscopy, molecular structures and interactions can be studied under physiological conditions shedding light on the structural underpinning of biological activity.
journal_name
J Proteomicsjournal_title
Journal of proteomicsauthors
Breindel L,Burz DS,Shekhtman Adoi
10.1016/j.jprot.2018.02.006subject
Has Abstractpub_date
2019-01-16 00:00:00pages
202-211eissn
1874-3919issn
1876-7737pii
S1874-3919(18)30055-1journal_volume
191pub_type
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journal_title:Journal of proteomics
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journal_title:Journal of proteomics
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doi:10.1016/j.jprot.2011.03.028
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journal_title:Journal of proteomics
pub_type: 杂志文章
doi:10.1016/j.jprot.2012.05.006
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journal_title:Journal of proteomics
pub_type: 杂志文章
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journal_title:Journal of proteomics
pub_type: 杂志文章
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