[ASAP] Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
Lysine Side-Chain Dynamics in the Binding Site of Homeodomain/DNA Complexes As Observed by NMR Relaxation Experiments and Molecular Dynamics Simulations
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00195/20180430/images/medium/bi-2018-001959_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00195
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/609FbT_MCUM
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05-01-2018 10:57 PM
[ASAP] Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-Resolution 31P Field-Cycling NMR Relaxometry
Dynamic Characteristics of Guanosine-5'-monophosphate Reductase Complexes Revealed by High-Resolution 31P Field-Cycling NMR Relaxometry
https://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.8b00142/20180326/images/medium/bi-2018-00142a_0007.gif
Biochemistry
DOI: 10.1021/acs.biochem.8b00142
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http://feeds.feedburner.com/~r/acs/bichaw/~4/VQwUOLCJfLo
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03-27-2018 06:28 AM
[NMR paper] 1H-NMR-Based Global Metabolic Studies of Pseudomonas aeruginosa upon Exposure of the Quorum Sensing Inhibitor Resveratrol.
1H-NMR-Based Global Metabolic Studies of Pseudomonas aeruginosa upon Exposure of the Quorum Sensing Inhibitor Resveratrol.
Related Articles 1H-NMR-Based Global Metabolic Studies of Pseudomonas aeruginosa upon Exposure of the Quorum Sensing Inhibitor Resveratrol.
J Proteome Res. 2017 Jan 17;:
Authors: Chen T, Sheng J, Fu Y, Li MH, Wang JS, Jia A
Abstract
Quorum sensing (QS) is a process of bacterial communication that has been a novel target for drug discovery. Pyocyanin quantification assay confirmed that resveratrol was an...
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01-19-2017 08:56 AM
Correction for Li et al., Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion [Correction]
Correction for Li et al., Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion
...
Date: 2013-11-26
BIOPHYSICS AND COMPUTATIONAL BIOLOGY Correction for “Mechanism of E-cadherin dimerization probed by NMR relaxation dispersion,” by Ying Li, Nicole L. Altorelli, Fabiana Bahna, Barry Honig, Lawrence Shapiro, and Arthur G. Palmer III, which appeared in issue 41, October 8, 2013, of Proc Natl Acad Sci USA (110:16462–16467; first published September... Read More
PNAS:
Number: 48
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11-27-2013 01:50 AM
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution
Abstract Random coil chemical shifts are necessary for secondary chemical shift analysis, which is the main NMR method for identification of secondary structure in proteins. One of the largest challenges in the determination of random coil chemical shifts is accounting for the effect of neighboring residues. The contributions from the neighboring residues are typically removed by using neighbor correction factors determined based on each...
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06-06-2011 12:53 AM
[NMR paper] NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: cha
NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
Related Articles NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
J Mol Recognit. 2001 May-Jun;14(3):166-71
Authors: Song J, Markley JL
The substrate-like...
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11-19-2010 08:32 PM
[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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11-17-2010 11:06 PM
[NMR paper] The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor is
The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The three-dimensional solution structure by 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata.
J Mol Biol. 1994 Sep 23;242(3):231-43
Authors: Nielsen KJ, Heath RL, Anderson MA, Craik DJ
The three-dimensional structure and disulfide connectivities of a 6-kDa...
![[ASAP] Correction to “Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase”](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-correction-%93inhibitor-complexes-pseudomonas-serine-carboxyl-proteinase%94_ltr.gif)
[ASAP] Correction to “Inhibitor Complexes of the Pseudomonas Serine-Carboxyl Proteinase”
Linear Mode
