Distribution of PASTA domains in penicillin-binding proteins and serine ... - Nature.com
Distribution of PASTA domains in penicillin-binding proteins and serine ... - Nature.com
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 ...
[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.
Related Articles Solution NMR assignment of LpoB, an outer-membrane anchored Penicillin-Binding Protein activator from Escherichia coli.
Biomol NMR Assign. 2014 Apr 2;
Authors: Jean NL, Bougault CM, Egan AJ, Vollmer W, Simorre JP
Abstract
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] ?-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study.
?-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study.
?-Sheet Nanocrystalline Domains Formed from Phosphorylated Serine-Rich Motifs in Caddisfly Larval Silk: A Solid State NMR and XRD Study.
Biomacromolecules. 2013 Mar 4;
Authors: Addison JB, Ashton NN, Weber WS, Stewart RJ, Holland GP, Yarger JL
Abstract
Adhesive silks spun by aquatic caddisfly (order Trichoptera) larvae are used to build both intricate protective shelters and food harvesting nets...
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[NMR paper] NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding reg
NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.
Related Articles NMR studies of internal dynamics of serine proteinase protein inhibitors: Binding region mobilities of intact and reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor (CMTI)-III of the squash family and comparison with those of counterparts of CMTI-V of the potato I family.
...
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[NMR paper] Orientational distribution of alpha-helices in the colicin B and E1 channel domains:
Orientational distribution of alpha-helices in the colicin B and E1 channel domains: a one and two dimensional 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers.
Related Articles Orientational distribution of alpha-helices in the colicin B and E1 channel domains: a one and two dimensional 15N solid-state NMR investigation in uniaxially aligned phospholipid bilayers.
Biochemistry. 1998 Jan 6;37(1):16-22
Authors: Lambotte S, Jasperse P, Bechinger B
Thermolytic fragments of the channel-forming bacterial toxins colicin...
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NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi1008535/aop/images/medium/bi-2010-008535_0002.gif
Biochemistry
DOI: 10.1021/bi1008535
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Related Articles NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Biochemistry. 2010 Aug 27;
Authors: Fatemi N, Korzhnev DM, VÄ?lyvis A, Sarkar B, Forman-Kay JD
The Wilson disease protein (ATP7B) is a copper-transporting member of the P-type ATPase superfamily, which plays a central role in copper homeostasis and interacts with the copper chaperone Atox1. The N-terminus of ATP7B is comprised of six copper-binding domains (WCBDs), each capable of binding one copper atom in the...
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[NMR paper] NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the D
NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific uridine substitutions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with...
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[NMR paper] NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the D
NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific uridine substitutions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with...