[ASAP] Rational Design of Monodispersed Mutants of Proteins by Identifying Aggregation Contact Sites Using Solubilizing Agents
Rational Design of Monodispersed Mutants of Proteins by Identifying Aggregation Contact Sites Using Solubilizing Agents
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00414/20200921/images/medium/bi0c00414_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00414
http://feeds.feedburner.com/~r/acs/bichaw/~4/04EE2_i8i74
More...
nmrlearner
Journal club
0
09-24-2020 07:17 PM
[NMR paper] Easy-to-Attach/Detach Solubilizing Tag-Aided Chemical Synthesis of an Aggregative Capsid Protein
Easy-to-Attach/Detach Solubilizing Tag-Aided Chemical Synthesis of an Aggregative Capsid Protein
A solubilizing "Trt-K10" tag was developed for the effective chemical preparation of peptides/proteins with low solubility. The Trt-K10 tag comprises a hydrophilic oligo-Lys sequence and a trityl anchor, and can be selectively introduced to a side chain thiol of Cys of deprotected peptides/proteins with a trityl alcohol-type introducing reagent "Trt(OH)-K10" under acidic conditions. Significantly, the ligation product in the reaction mixture of a thiol-additive-free native chemical ligation...
nmrlearner
Journal club
0
01-09-2018 09:41 AM
[NMR paper] Palladium in the Chemical Synthesis and Modification of Proteins
Palladium in the Chemical Synthesis and Modification of Proteins
The field of site-specific modification of proteins has drawn significant attention in recent years owing to its importance in various research areas such as the development of novel therapeutics and understanding the biochemical and cellular behaviors of proteins. The presence of a large number of reactive functional groups in the protein of interest and in the cellular environment renders modification at a specific site a highly challenging task. With the development of sophisticated chemical methodologies it is now...
nmrlearner
Journal club
0
08-07-2017 07:31 PM
Fractional enrichment of proteins using [2- 13 C]-glycerol as the carbon source facilitates measurement of excited state 13 Cα chemical shifts with improved sensitivity
Fractional enrichment of proteins using -glycerol as the carbon source facilitates measurement of excited state 13 Cα chemical shifts with improved sensitivity
Abstract
A selective isotope labeling scheme based on the utilization of -glycerol as the carbon source during protein overexpression has been evaluated for the measurement of excited state 13Cα chemical shifts using Carrâ??Purcellâ??Meiboomâ??Gill (CPMG) relaxation dispersion (RD) experiments. As expected, the fractional incorporation of label at the Cα positions is increased two-fold...
nmrlearner
Journal club
0
05-20-2015 10:27 AM
[NMR paper] The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media.
The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media.
Related Articles The Use of Amphipols for Solution NMR Studies of Membrane Proteins: Advantages and Constraints as Compared to Other Solubilizing Media.
J Membr Biol. 2014 Mar 28;
Authors: Planchard N, Point E, Dahmane T, Giusti F, Renault M, Le Bon C, Durand G, Milon A, Guittet E, Zoonens M, Popot JL, Catoire LJ
Abstract
Solution-state nuclear magnetic resonance studies of membrane proteins are...
nmrlearner
Journal club
0
03-29-2014 01:00 PM
[NMR paper] An 1H NMR determination of the three-dimensional structures of mirror-image forms of
An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] An 1H NMR determination of the three-dimensional structures of mirror-image forms of
An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium elaterium (EETI-II).
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles An 1H NMR determination of the three-dimensional structures of mirror-image forms of a Leu-5 variant of the trypsin inhibitor from Ecballium...
An Enzyme-Cleavable Solubilizing-Tag Facilitates the Chemical Synthesis of Mirror-Image Proteins
Linear Mode
