| Autor: |
Ji Lv, Yan Jin, Jin Chen, Ye Zhou, Zheyi Liu, Lin Liu, Fangjun Wang, Binwen Sun |
| Rok vydání: |
2021 |
| Předmět: |
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| Zdroj: |
Analytical chemistry. 93(30) |
| ISSN: |
1520-6882 |
| Popis: |
Monitoring the dynamic alterations of protein structures within an aqueous solution remains enormously challenging. In this study, we describe a size-selective VAILase proteolysis (SVP)-mass spectrometry (MS) strategy to probe the protein structure changes without strict control of the proteolysis kinetics. The unique conformation selectivity of SVP depends on the uniform nano-sized entrance pores of the VAILase hexameric cage as well as the six inherent molecular rulers in the VAILase-substrate recognition and cleavage. The dynamic insights into subtle conformation alterations of both myoglobin unfolding transition and Aurora kinase A-inhibitor binding are successfully captured using the SVP strategy, which matches well with the results in the molecular dynamics simulation. Our work provides a new paradigm of size-selective native proteolysis for exploring the aqueous protein structure-function relationships. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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