[ASAP] Protein Splicing Activity of the Haloferax volcanii PolB-c Intein Is Sensitive to Homing Endonuclease Domain Mutations
Protein Splicing Activity of the Haloferax volcanii PolB-c Intein Is Sensitive to Homing Endonuclease Domain Mutations
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00512/20200902/images/medium/bi0c00512_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00512
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nmrlearner
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09-13-2020 09:18 AM
[ASAP] Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein
Allosteric Influence of Extremophile Hairpin Motif Mutations on the Protein Splicing Activity of a Hyperthermophilic Intein
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00348/20200624/images/medium/bi0c00348_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00348
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nmrlearner
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06-25-2020 02:58 AM
[ASAP] Identification of the Functional Roles of Six Key Proteins in the Biosynthesis of Enterobacteriaceae Colanic Acid
Identification of the Functional Roles of Six Key Proteins in the Biosynthesis of Enterobacteriaceae Colanic Acid
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00040/20190312/images/medium/bi-2019-00040b_0001.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00040
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http://feeds.feedburner.com/~r/acs/bichaw/~4/5V8t--GzQSM
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nmrlearner
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03-24-2019 10:41 PM
[ASAP] Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2
Post-Translational Modifications in Polypyrimidine Tract Binding Proteins PTBP1 and PTBP2
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00256/20180613/images/medium/bi-2018-00256v_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00256
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http://feeds.feedburner.com/~r/acs/bichaw/~4/EbXJowbwGpU
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nmrlearner
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06-14-2018 08:12 AM
[ASAP] Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems
Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01275/20180404/images/medium/bi-2017-012754_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01275
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http://feeds.feedburner.com/~r/acs/bichaw/~4/RiC9C-kPHns
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nmrlearner
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04-06-2018 01:51 AM
[ASAP] Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein
Bacterial Model Membranes Reshape Fibrillation of a Functional Amyloid Protein
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00002/20180402/images/medium/bi-2018-00002f_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00002
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http://feeds.feedburner.com/~r/acs/bichaw/~4/IKrC6FWKK6c
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nmrlearner
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04-03-2018 05:04 AM
Identification of a Conserved Histidine As Being Criticalfor the Catalytic Mechanism and Functional Switching of the MultifunctionalProline Utilization A Protein
Identification of a Conserved Histidine As Being Criticalfor the Catalytic Mechanism and Functional Switching of the MultifunctionalProline Utilization A Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00046/20170608/images/medium/bi-2017-00046v_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00046
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nmrlearner
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06-09-2017 09:13 AM
[NMR paper] NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in so
NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Related Articles NMR characterization of the Escherichia coli nitrogen regulatory protein IIANtr in solution and interaction with its partner protein, NPr.
Protein Sci. 2005 Apr;14(4):1082-90
Authors: Wang G, Peterkofsky A, Keifer PA, Li X
The solution form of IIA(Ntr) from Escherichia coli and its interaction with its partner protein, NPr, were characterized by nuclear magnetic resonance (NMR)...