[ASAP] Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein
[ASAP] Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein
[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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nmrlearner
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04-06-2018 01:51 AM
Mode of Interaction of the Signal-Transducing ProteinEIIAGlc with the Maltose ABC Transporter in the Processof Inducer Exclusion
Mode of Interaction of the Signal-Transducing ProteinEIIAGlc with the Maltose ABC Transporter in the Processof Inducer Exclusion
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00721/20160919/images/medium/bi-2016-007219_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00721
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nmrlearner
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09-22-2016 06:22 AM
[NMR paper] The energetic cost of domain reorientation in maltose-binding protein as studied by N
The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy.
Related Articles The energetic cost of domain reorientation in maltose-binding protein as studied by NMR and fluorescence spectroscopy.
Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12700-5
Authors: Millet O, Hudson RP, Kay LE
Maltose-binding protein (MBP) is a two-domain protein that undergoes a ligand-mediated conformational rearrangement from an "open" to a "closed" structure on binding to maltooligosaccharides. To...
nmrlearner
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11-24-2010 09:16 PM
[NMR paper] 19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesi
19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues.
Related Articles 19F NMR study of the leucine-specific binding protein of Escherichia coli: mutagenesis and assignment of the 5-fluorotryptophan-labeled residues.
Protein Eng. 2002 Nov;15(11):855-9
Authors: Salopek-Sondi B, Luck LA
The Escherichia coli L-leucine receptor is an aqueous protein and the first component in the distinct transport pathway for hydrophobic amino acids. L-leucine binding...
nmrlearner
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11-24-2010 08:58 PM
[NMR paper] Detection of a conformational change in maltose binding protein by (129)Xe NMR spectr
Detection of a conformational change in maltose binding protein by (129)Xe NMR spectroscopy.
Related Articles Detection of a conformational change in maltose binding protein by (129)Xe NMR spectroscopy.
J Am Chem Soc. 2001 Sep 5;123(35):8616-7
Authors: Rubin SM, Spence MM, Dimitrov IE, Ruiz EJ, Pines A, Wemmer DE
nmrlearner
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11-19-2010 08:44 PM
[NMR paper] Identification of the DNA binding surface of H-NS protein from Escherichia coli by he
Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
Related Articles Identification of the DNA binding surface of H-NS protein from Escherichia coli by heteronuclear NMR spectroscopy.
FEBS Lett. 1999 Jul 16;455(1-2):63-9
Authors: Shindo H, Ohnuki A, Ginba H, Katoh E, Ueguchi C, Mizuno T, Yamazaki T
The DNA binding domain of H-NS protein was studied with various N-terminal deletion mutant proteins and identified by gel retardation assay and heteronuclear 2D- and 3D-NMR...
nmrlearner
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11-18-2010 08:31 PM
[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
...
nmrlearner
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08-22-2010 03:31 PM
[NMR paper] Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Related Articles Tritium NMR spectroscopy of ligand binding to maltose-binding protein.
Biochemistry. 1991 Jun 4;30(22):5524-31
Authors: Gehring K, Williams PG, Pelton JG, Morimoto H, Wemmer DE
Tritium-labeled alpha- and beta-maltodextrins have been used to study their complexes with maltose-binding protein (MBP), a 40-kDa bacterial protein. Five substrates, from maltose to maltohexaose, were labeled at their reducing ends and their binding studied. Tritium NMR spectroscopy...
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[ASAP] Conformational Dynamics in the Binding-Protein-Independent Mutant of the Escherichia coli Maltose Transporter, MalG511, and Its Interaction with Maltose Binding Protein
Linear Mode
