SilE and SilB are both proteins involved in the silver efflux pump found in Gram-negative bacteria such as S. typhimurium. Using model peptides along with NMR and CD experiments, we show how SilE may store silver ions prior to delivery and we hypothesize for the first time the interplay between SilB and SilE.
Pressure dependence of side chain 1 H and 15 N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of side chain 1 H and 15 N-chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For interpreting the pressure induced shifts of resonance lines of folded as well as unfolded proteins the availability of data from well-defined model systems is indispensable. Here, we report the pressure dependence of 1H and 15N chemical shifts of the side chain atoms in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx is one of the 20 canonical amino acids) measured at 800Â*MHz proton frequency. As observed earlier for other...
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06-22-2020 10:19 PM
[NMR paper] NMR metabolomics reveals metabolism-mediated protective effects in liver (HepG2) cells exposed to sub-toxic levels of silver nanoparticles.
NMR metabolomics reveals metabolism-mediated protective effects in liver (HepG2) cells exposed to sub-toxic levels of silver nanoparticles.
NMR metabolomics reveals metabolism-mediated protective effects in liver (HepG2) cells exposed to sub-toxic levels of silver nanoparticles.
J Proteome Res. 2018 Mar 02;:
Authors: Carrola J, Pinto RJB, Nasirpour M, Freire CSR, Gil AM, Santos C, Oliveira H, Duarte IF
Abstract
The expansion of biomedical and therapeutic applications of silver nanoparticles (AgNPs) raises the need to further...
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03-03-2018 12:01 PM
Overall Structural Model of NS5A Protein from HepatitisC Virus and Modulation by Mutations Confering Resistance of VirusReplication to Cyclosporin A
Overall Structural Model of NS5A Protein from HepatitisC Virus and Modulation by Mutations Confering Resistance of VirusReplication to Cyclosporin A
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00212/20170607/images/medium/bi-2017-00212h_0013.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00212
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/iHH6K9n1w0Q
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06-08-2017 03:17 AM
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Pressure dependence of backbone chemical shifts in the model peptides Ac-Gly-Gly-Xxx-Ala-NH 2
Abstract
For a better understanding of nuclear magnetic resonance (NMR) detected pressure responses of folded as well as unstructured proteins the availability of data from well-defined model systems are indispensable. In this work we report the pressure dependence of chemical shifts of the backbone atoms 1Hα, 13Cα and 13C� in the protected tetrapeptides Ac-Gly-Gly-Xxx-Ala-NH2 (Xxx one of the 20 canonical amino acids). Contrary to...
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06-22-2016 09:14 PM
CD and NMR investigation of collagen peptides mimicking a pathological Gly–Ser mutation and a natural interruption in a similar highly charged sequence context
CD and NMR investigation of collagen peptides mimicking a pathological Gly–Ser mutation and a natural interruption in a similar highly charged sequence context
Abstract
Even a single Gly substitution in the triple helix domain of collagen leads to pathological conditions while natural interruptions are suggested to play important functional roles. Two peptides—one mimicking a pathological Gly–Ser substitution (ERSEQ) and the other one modeling a similar natural interruption sequence (DRSER)—are designed to facilitate the comparison for elucidating the molecular basis of their different...
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11-27-2015 04:49 PM
[NMR paper] CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context.
Protein Sci. 2015 Oct 12;
Authors: Sun X, Liu S, Yu W, Wang S, Xiao J
Abstract
Even a single Gly substitution in the triple helix domain of collagen leads to pathological conditions, while natural interruptions...
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10-13-2015 06:03 PM
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context
CD and NMR investigation of collagen peptides mimicking a pathological Gly-Ser mutation and a natural interruption in a similar highly charged sequence context
ABSTRACT
Even a single Gly substitution in the triple helix domain of collagen leads to pathological conditions, while natural interruptions are suggested to play important functional roles. Two peptides, one mimicking a pathological Gly-Ser substitution (ERSEQ) and the other one modeling a similar natural interruption sequence (DRSER), are designed to facilitate the comparison for elucidating the molecular basis of their...
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10-13-2015 05:51 AM
[Question from NMRWiki Q&A forum] Please suggest model proteins and peptides for NMR
Please suggest model proteins and peptides for NMR
do you know any model proteins except lysozyme suitable for nmr experiments?
Check if somebody has answered this question on NMRWiki QA forum
NMR reveals the interplay between SilE and SilB model peptides in the context of silver resistance
Linear Mode
