In:
Angewandte Chemie, Wiley, Vol. 131, No. 37 ( 2019-09-09), p. 13103-13107
Abstract:
Elucidating at atomic level how proteins interact and are chemically modified in cells represents a leading frontier in structural biology. We have developed a tailored solid‐state NMR spectroscopic approach that allows studying protein structure inside human cells at atomic level under high‐sensitivity dynamic nuclear polarization (DNP) conditions. We demonstrate the method using ubiquitin (Ub), which is critically involved in cellular functioning. Our results pave the way for structural studies of larger proteins or protein complexes inside human cells, which have remained elusive to in‐cell solution‐state NMR spectroscopy due to molecular size limitations.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v131.37
DOI:
10.1002/ange.201903246
Language:
English
Publisher:
Wiley
Publication Date:
2019
detail.hit.zdb_id:
505868-5
detail.hit.zdb_id:
506609-8
detail.hit.zdb_id:
514305-6
detail.hit.zdb_id:
505872-7
detail.hit.zdb_id:
1479266-7
detail.hit.zdb_id:
505867-3
detail.hit.zdb_id:
506259-7
Permalink