| Autor: |
Rongfu Zhang, Timothy A. Cross, Riqiang Fu |
| Jazyk: |
angličtina |
| Rok vydání: |
2021 |
| Předmět: |
|
| Zdroj: |
Magnetic Resonance Letters, Vol 1, Iss 2, Pp 99-111 (2021) |
| Druh dokumentu: |
article |
| ISSN: |
2772-5162 |
| DOI: |
10.1016/j.mrl.2021.09.002 |
| Popis: |
Water plays an important role in many essential biological processes of membrane proteins in hydrated lipid environments. In general, the 1H polarization transfers between water molecules and site-specific protons in proteins can be classified as coherent (via dipolar spin diffusion) and incoherent (via chemical exchange and nuclear Overhauser effect) transfers. Solid-state NMR is the technique of choice for studying such water-protein interactions in membrane-bound proteins/peptides through the detection of 1H polarization transfers from water to the proteins. These polarization transfer mechanisms often exist simultaneously and are difficult to quantify individually. Here, we review water-protein polarization transfer techniques in solid-state NMR, with a focus on the recent progress for the direct detection of site-specific kinetic water-protein chemical exchange processes on the sub-millisecond time scale in membrane-bound proteins. The measurements of the pure chemical exchange kinetics provide a unique opportunity to understand the role that water plays in the structure-function relationships of membrane-bound species at the water-bilayer interface. In addition, the perspective of chemical exchange saturation transfer (CEST) experiments in membrane-bound proteins/peptides is further discussed. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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