Quantitative mass imaging of single biological macromolecules.
Science
; 360(6387): 423-427, 2018 04 27.
Article
em En
| MEDLINE
| ID: mdl-29700264
ABSTRACT
The cellular processes underpinning life are orchestrated by proteins and their interactions. The associated structural and dynamic heterogeneity, despite being key to function, poses a fundamental challenge to existing analytical and structural methodologies. We used interferometric scattering microscopy to quantify the mass of single biomolecules in solution with 2% sequence mass accuracy, up to 19-kilodalton resolution, and 1-kilodalton precision. We resolved oligomeric distributions at high dynamic range, detected small-molecule binding, and mass-imaged proteins with associated lipids and sugars. These capabilities enabled us to characterize the molecular dynamics of processes as diverse as glycoprotein cross-linking, amyloidogenic protein aggregation, and actin polymerization. Interferometric scattering mass spectrometry allows spatiotemporally resolved measurement of a broad range of biomolecular interactions, one molecule at a time.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Polimerização
/
Agregação Patológica de Proteínas
/
Imagem Individual de Molécula
/
Microscopia de Interferência
Idioma:
En
Ano de publicação:
2018
Tipo de documento:
Article