NMR Methods to Study Dynamic Allostery.
Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2016-03-01
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| Series: | PLoS Computational Biology |
| Online Access: | http://europepmc.org/articles/PMC4786136?pdf=render |
| _version_ | 1818291328968032256 |
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| author | Sarina Grutsch Sven Brüschweiler Martin Tollinger |
| author_facet | Sarina Grutsch Sven Brüschweiler Martin Tollinger |
| author_sort | Sarina Grutsch |
| collection | DOAJ |
| description | Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at unprecedented detail, revealing intriguing aspects of allosteric mechanisms and increasing the proportion of the conformational ensemble that can be observed by experiment. Here, we present an overview of NMR spectroscopic methods for characterizing equilibrium fluctuations in free and bound states of allosteric proteins that have been most influential in the field. By combining NMR experimental approaches with molecular simulations, atomistic-level descriptions of the mechanisms by which allosteric phenomena take place are now within reach. |
| first_indexed | 2024-12-13T02:42:20Z |
| format | Article |
| id | doaj.art-bbb0db341c63436cb56ac9de0d55aab7 |
| institution | Directory Open Access Journal |
| issn | 1553-734X 1553-7358 |
| language | English |
| last_indexed | 2024-12-13T02:42:20Z |
| publishDate | 2016-03-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Computational Biology |
| spelling | doaj.art-bbb0db341c63436cb56ac9de0d55aab72022-12-22T00:02:17ZengPublic Library of Science (PLoS)PLoS Computational Biology1553-734X1553-73582016-03-01123e100462010.1371/journal.pcbi.1004620NMR Methods to Study Dynamic Allostery.Sarina GrutschSven BrüschweilerMartin TollingerNuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at unprecedented detail, revealing intriguing aspects of allosteric mechanisms and increasing the proportion of the conformational ensemble that can be observed by experiment. Here, we present an overview of NMR spectroscopic methods for characterizing equilibrium fluctuations in free and bound states of allosteric proteins that have been most influential in the field. By combining NMR experimental approaches with molecular simulations, atomistic-level descriptions of the mechanisms by which allosteric phenomena take place are now within reach.http://europepmc.org/articles/PMC4786136?pdf=render |
| spellingShingle | Sarina Grutsch Sven Brüschweiler Martin Tollinger NMR Methods to Study Dynamic Allostery. PLoS Computational Biology |
| title | NMR Methods to Study Dynamic Allostery. |
| title_full | NMR Methods to Study Dynamic Allostery. |
| title_fullStr | NMR Methods to Study Dynamic Allostery. |
| title_full_unstemmed | NMR Methods to Study Dynamic Allostery. |
| title_short | NMR Methods to Study Dynamic Allostery. |
| title_sort | nmr methods to study dynamic allostery |
| url | http://europepmc.org/articles/PMC4786136?pdf=render |
| work_keys_str_mv | AT sarinagrutsch nmrmethodstostudydynamicallostery AT svenbruschweiler nmrmethodstostudydynamicallostery AT martintollinger nmrmethodstostudydynamicallostery |