Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1016/j.jmb.2020.10.025 http://scihub22266oqcxt.onion/10.1016/j.jmb.2020.10.025 33203509!7611467!33203509     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33203509&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       J+Mol+Biol 2021 ; 433 (17): 166691 Nephropedia Template TP {{tp|p=33203509|t=2021. Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence |pdf=|usr=}}{{33203509}} gab.com Text Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence JO: J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33203509 #FOAvip Magnesium is the most abundant divalent cation present in the cell, and an abnormal Mg(2+) homeostasis is associated with several diseases in humans. However, among ion channels, the mechanisms of intracellular regulation and transport of Mg(2+) are poorly understood. MgtE is a homodimeric Mg(2+)-selective channel and is negatively regulated by high intracellular Mg(2+) concentration where the cytoplasmic domain of MgtE acts as a Mg(2+) sensor. Most of the previous biophysical studies on MgtE have been carried out in detergent micelles and the information regarding gating-related structural dynamics of MgtE in physiologically-relevant membrane environment is scarce. In this work, we monitored the changes in gating-related structural dynamics, hydration dynamics and conformational heterogeneity of MgtE in micelles and membranes using the intrinsic site-directed Trp fluorescence. For this purpose, we have engineered six single-Trp mutants in the functional Trp-less background of MgtE to obtain site-specific information on the gating-related structural dynamics of MgtE in membrane-mimetic systems. Our results indicate that Mg(2+)-induced gating might involve the possibility of a 'conformational wave' from the cytosolic N-domain to transmembrane domain of MgtE. Although MgtE is responsive to Mg(2+)-induced gating in both micelles and membranes, the organization and dynamics of MgtE is substantially altered in physiologically important phospholipid membranes compared to micelles. This is accompanied by significant changes in hydration dynamics and conformational heterogeneity. Overall, our results highlight the importance of lipid-protein interactions and are relevant for understanding gating mechanism of magnesium channels in general, and MgtE in particular. Twit Text FOAVip Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence ????J Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33203509 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33203509 #FOAvip English Wikipedia <ref>{{Cite pmid|33203509}}</ref> Gating-related Structural Dynamics of the MgtE Magnesium Channel in Membrane-Mimetics Utilizing Site-Directed Tryptophan Fluorescence #MMPMID33203509 Chatterjee S; Brahma R; Raghuraman H J Mol Biol 2021[Aug]; 433 (17): 166691 PMID33203509show ga Magnesium is the most abundant divalent cation present in the cell, and an abnormal Mg(2+) homeostasis is associated with several diseases in humans. However, among ion channels, the mechanisms of intracellular regulation and transport of Mg(2+) are poorly understood. MgtE is a homodimeric Mg(2+)-selective channel and is negatively regulated by high intracellular Mg(2+) concentration where the cytoplasmic domain of MgtE acts as a Mg(2+) sensor. Most of the previous biophysical studies on MgtE have been carried out in detergent micelles and the information regarding gating-related structural dynamics of MgtE in physiologically-relevant membrane environment is scarce. In this work, we monitored the changes in gating-related structural dynamics, hydration dynamics and conformational heterogeneity of MgtE in micelles and membranes using the intrinsic site-directed Trp fluorescence. For this purpose, we have engineered six single-Trp mutants in the functional Trp-less background of MgtE to obtain site-specific information on the gating-related structural dynamics of MgtE in membrane-mimetic systems. Our results indicate that Mg(2+)-induced gating might involve the possibility of a 'conformational wave' from the cytosolic N-domain to transmembrane domain of MgtE. Although MgtE is responsive to Mg(2+)-induced gating in both micelles and membranes, the organization and dynamics of MgtE is substantially altered in physiologically important phospholipid membranes compared to micelles. This is accompanied by significant changes in hydration dynamics and conformational heterogeneity. Overall, our results highlight the importance of lipid-protein interactions and are relevant for understanding gating mechanism of magnesium channels in general, and MgtE in particular. |Bacterial Proteins/metabolism[MESH] |Dimerization[MESH] |Fluorescence[MESH] |Homeostasis/physiology[MESH] |Ion Channels/*metabolism[MESH] |Magnesium/*metabolism[MESH] |Membranes/*metabolism[MESH] |Protein Domains/physiology[MESH] |Thermus thermophilus/metabolism[MESH]Gating-related Structural Dynamics of the MgtE Magnesium Channel in M(epmc).pdf DeepDyve Pubget Overpricing