| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T714 |
0-28 |
Sentence |
denotes |
4.4. “In-Virus” NMR Strategy |
| T715 |
29-244 |
Sentence |
denotes |
In many viruses and phages, scaffolding proteins (SPs) are required to ensure the correct organization of coat proteins (CPs) and other minor capsid proteins into a precursor structure, called a procapsid [428,429]. |
| T716 |
245-423 |
Sentence |
denotes |
Although SPs are critical for viral assembly and therefore potential therapeutic targets their structural properties (with only a few exceptions [430,431]) are poorly understood. |
| T717 |
424-574 |
Sentence |
denotes |
The size limitation of NMR can be used advantageously as a filter to identify disordered segments even in very large supramolecular protein complexes. |
| T718 |
575-717 |
Sentence |
denotes |
In this way, NMR can provide a unique perspective on the dynamic and disordered elements of macromolecules not accessible by other techniques. |
| T719 |
718-1127 |
Sentence |
denotes |
The procapsid encapsulation experiments described by Whitehead et al. [432] were conceptually analogous to in-cell NMR experiments [433,434,435] in which signals from small proteins, or flexible segments of proteins, can be observed when they are incorporated inside living cells, as long as the isotope-labeled proteins of interest do not interact strongly with other large cellular components [433,434,435]. |
| T720 |
1128-1399 |
Sentence |
denotes |
The so called ‘‘in-virus’’ NMR strategy applied by Whitehead et al. [432] could be more generally used to study the dynamic properties of macromolecules encapsulated into virus particles, including cargo molecules encased in viral capsids for nanotechnology applications. |
| T721 |
1400-1551 |
Sentence |
denotes |
Additionally, such studies could assess the level of interaction of cargo molecules with the virus and probe the release properties of cargo NMR [432]. |
