Synthesis and Kinetic Analysis of Two ConformationallyRestricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5
Synthesis and Kinetic Analysis of Two ConformationallyRestricted Peptide Substrates of Escherichia coli Penicillin-Binding Protein 5
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Biochemistry
DOI: 10.1021/acs.biochem.6b00576
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Distribution of PASTA domains in penicillin-binding proteins and serine ... - Nature.com
Distribution of PASTA domains in penicillin-binding proteins and serine ... - Nature.com
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Distribution of PASTA domains in penicillin-binding proteins and serine ...
Nature.com
PASTA domains (penicillin-binding protein and serine/threonine kinase-associated domains) have been identified in penicillin-binding proteins and serine/threonine kinases of Gram-positive Firmicutes and Actinobacteria. ..... When the secondary and ...
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[NMR paper] J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4.
J Biomol NMR. 2014 Nov 27;
Authors: Jaudzems K, Pedrini B, Geralt M, Serrano P, Wüthrich K
Abstract
The NMR structure of the 206-residue protein NP_346487.1 was determined with the J-UNIO protocol, which includes extensive automation of the structure determination. With input...
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11-28-2014 11:37 AM
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4
J-UNIO protocol used for NMR structure determination of the 206-residue protein NP_346487.1 from Streptococcus pneumoniae TIGR4
Abstract
The NMR structure of the 206-residue protein NP_346487.1 was determined with the J-UNIO protocol, which includes extensive automation of the structure determination. With input from three APSY-NMR experiments, UNIO-MATCH automatically yielded 77Â*% of the backbone assignments, which were interactively validated and extended to 97Â*%. With an input of the near-complete backbone assignments and three 3D...
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11-26-2014 10:50 PM
[NMR paper] NMR assignment of the amylase-binding protein A from Streptococcus parasanguinis.
NMR assignment of the amylase-binding protein A from Streptococcus parasanguinis.
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Biomol NMR Assign. 2014 Jul 14;
Authors: Liu B, Zhu F, Wu H, Matthews S
Abstract
Streptococcus parasanguinis is a primary colonizer of tooth surfaces in the oral cavity. Amylase-binding protein A (AbpA) from S. parasanguinis is responsible for the recruitment of salivary amylase to bacterial surface, which plays an important role in the...
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[NMR paper] Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
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Biomol NMR Assign. 2014 Apr 2;
Authors: Jean NL, Bougault CM, Egan AJ, Vollmer W, Simorre JP
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Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to...
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[NMR paper] Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_npg.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the Big domain from Streptococcus pneumoniae reveals a novel Ca(2+)-binding module.
Sci Rep. 2013;3:1079
Authors: Wang T, Zhang J, Zhang X, Xu C, Tu X
Abstract
Streptococcus pneumoniae is a...
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[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche
An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Related Articles An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Biochemistry. 1994 Jul 26;33(29):8651-61
Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C
Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...