Correction to Structure of a Novel Phosphotriesterasefrom Sphingobium sp. TCM1: A Familiar Binuclear Metal Center Embedded in a Seven-Bladed ?-Propeller Protein Fold
Correction to Structure of a Novel Phosphotriesterasefrom Sphingobium sp. TCM1: A Familiar Binuclear Metal Center Embedded in a Seven-Bladed ?-Propeller Protein Fold
Structure of a Novel Phosphotriesterase from Sphingobium sp. TCM1: A Familiar Binuclear Metal CenterEmbedded in a Seven-Bladed ?-Propeller Protein Fold
Structure of a Novel Phosphotriesterase from Sphingobium sp. TCM1: A Familiar Binuclear Metal CenterEmbedded in a Seven-Bladed ?-Propeller Protein Fold
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00364/20160708/images/medium/bi-2016-00364c_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00364
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/8jtHt_1h0fU
More...
[NMR paper] Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.
Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.
Correction of erroneously packed protein's side chains in the NMR structure based on ab initio chemical shift calculations.
Phys Chem Chem Phys. 2014 Jul 23;
Authors: Zhu T, Zhang JZ, He X
Abstract
In this work, protein side chain (1)H chemical shifts are used as probes to detect and correct side-chain packing errors in protein's NMR structures through structural refinement. By applying the automated...
nmrlearner
Journal club
0
07-24-2014 11:56 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
nmrlearner
Journal club
0
11-27-2013 01:50 AM
[NMR paper] Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein.
Nat Methods. 2013 Sep 8;
Authors: Wang S, Munro RA, Shi L, Kawamura I, Okitsu T, Wada A, Kim SY, Jung KH, Brown LS, Ladizhansky V
Abstract
Determination of structure of integral membrane proteins, especially in their native environment, is a formidable challenge in structural biology. Here we demonstrate that magic angle spinning...
nmrlearner
Journal club
0
09-10-2013 08:44 PM
[NMR paper] Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
Related Articles Solution NMR refinement of a metal ion bound protein using metal ion inclusive restrained molecular dynamics methods.
J Biomol NMR. 2013 Apr 23;
Authors: Chakravorty DK, Wang B, Lee CW, Guerra AJ, Giedroc DP, Merz KM
Abstract
Correctly calculating the structure of metal coordination sites in a protein during the process of nuclear magnetic resonance (NMR) structure determination and refinement continues to...
nmrlearner
Journal club
0
04-24-2013 09:48 PM
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...
nmrlearner
Journal club
0
06-06-2011 12:53 AM
[NMR paper] Enhanced protein fold recognition using secondary structure information from NMR.
Enhanced protein fold recognition using secondary structure information from NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Enhanced protein fold recognition using secondary structure information from NMR.
Protein Sci. 1999 May;8(5):1127-33
Authors: Ayers DJ, Gooley PR, Widmer-Cooper A, Torda AE
NMR offers...
Correction to Structure of a Novel Phosphotriesterasefrom Sphingobium sp. TCM1: A Familiar Binuclear Metal Center Embedded in a Seven-Bladed ?-Propeller Protein Fold
Linear Mode
