[ASAP] Conserved Structural Motif Identified in Peptides That Bind to Geminivirus Replication Protein Rep
Conserved Structural Motif Identified in Peptides That Bind to Geminivirus Replication Protein Rep
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00408/20210831/images/medium/bi1c00408_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00408
http://feeds.feedburner.com/~r/acs/bichaw/~4/DkFk0O3oPso
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nmrlearner
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09-02-2021 02:00 AM
[NMR paper] The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR
The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1-248 residue construct: sequence-specific resonance assignments through NMR
The nucleocapsid protein N from SARS-CoV-2 is one of the most highly expressed proteins by the virus and plays a number of important roles in the transcription and assembly of the virion within the infected host cell. It is expected to be characterized by a highly dynamic and heterogeneous structure as can be inferred by bioinformatics analyses as well as from the data available for the homologous protein from SARS-CoV. The...
nmrlearner
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03-04-2021 12:41 PM
[ASAP] The Human Fragile X Mental Retardation Protein Inhibits the Elongation Step of Translation through Its RGG and C-Terminal Domains
The Human Fragile X Mental Retardation Protein Inhibits the Elongation Step of Translation through Its RGG and C-Terminal Domains
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00534/20200929/images/medium/bi0c00534_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00534
http://feeds.feedburner.com/~r/acs/bichaw/~4/yzpP4lQOuiA
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nmrlearner
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09-29-2020 07:53 PM
[ASAP] Both Ligands and Macromolecular Crowders Preferentially Bind to Closed Conformations of Maltose Binding Protein
Both Ligands and Macromolecular Crowders Preferentially Bind to Closed Conformations of Maltose Binding Protein
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b00154/20190412/images/medium/bi-2019-001548_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b00154
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/oQ3jllwp6Vo
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nmrlearner
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04-12-2019 05:25 PM
[ASAP] Target Engagement and Binding Mode of an Antituberculosis Drug to Its Bacterial Target Deciphered in Whole Living Cells by NMR
Target Engagement and Binding Mode of an Antituberculosis Drug to Its Bacterial Target Deciphered in Whole Living Cells by NMR
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00975/20190103/images/medium/bi-2018-00975t_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00975
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/J0ajkYKpz7s
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nmrlearner
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01-07-2019 05:49 AM
[ASAP] The “Recognition Helix” of the Type II Acyl Carrier Protein (ACP) Utilizes a “Ubiquitin Interacting Motif (UIM)”-like Surface To Bind Its Partners
The “Recognition Helix” of the Type II Acyl Carrier Protein (ACP) Utilizes a “Ubiquitin Interacting Motif (UIM)”-like Surface To Bind Its Partners
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00220/20180619/images/medium/bi-2018-00220e_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00220
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/4D50TNanhmQ
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nmrlearner
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06-19-2018 08:46 PM
[NMR paper] A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.
A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.
Related Articles A Method for Systematic Assessment of Intrinsically Disordered Protein Regions by NMR.
Int J Mol Sci. 2015;16(7):15743-15760
Authors: Goda N, Shimizu K, Kuwahara Y, Tenno T, Noguchi T, Ikegami T, Ota M, Hiroaki H
Abstract
Intrinsically disordered proteins (IDPs) that lack stable conformations and are highly flexible have attracted the attention of biologists. Therefore, the development of a systematic method to identify...