Related ArticlesAn efficient NMR experiment for analyzing sugar-puckering in unlabeled DNA: application to the 26-kDa dead ringer-DNA complex.
J Magn Reson. 2001 Dec;153(2):262-6
Authors: Iwahara J, Wojciak JM, Clubb RT
We present a new NMR experiment for estimating the type and degree of sugar-puckering in high-molecular-weight unlabeled DNA molecules. The experiment consists of a NOESY sequence preceded by a constant-time scalar coupling period. Two subexperiments are compared, each differing in the amount of time the (3)J(H3'H2') and (3)J(H3'H2") couplings are active on the H3' magnetization. The resultant data are easy to analyze, since a comparison of the signal intensities of any resolved NOE cross peak originating from H3' atoms of the duplex can be used to estimate the sum of the (3)J(H3'H2') and (3)J(H3'H2") couplings and thus the puckering type of the deoxyribose ring. Isotope filters to eliminate signals of the (13)C-labeled component in the F1-dimension are implemented, facilitating analyses of high-molecular-weight protein-DNA complexes containing (13)C-labeled protein and unlabeled DNA. The utility of the experiment is demonstrated on the 26-kDa Dead Ringer protein-DNA complex and reveals that the DNA uniformly adopts the S-type configuration when bound to protein.
Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ... - Genetic Engineering News
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Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ...
Genetic Engineering News
Bruker and Lawrence Berkeley National Laboratory are collaborating to develop structural biology methods and tools that integrate small-angle x-ray scattering (SAXS) technology with nuclear magnetic resonance (NMR). The aim is to generate a set of data ...
Bruker and Lawrence Berkeley National Laboratory Collaborate on Novel ...MarketWatch (press release)
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11-11-2011 08:26 AM
Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ... - Genetic Engineering News
Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ... - Genetic Engineering News
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Bruker and Berkeley Lab Combine NMR with SAXS for Analyzing Large Protein ...
Genetic Engineering News
The aim is to generate a set of data analysis algorithms for determining the structures of larger, multi-domain proteins and protein complexes with DNA, RNA or other proteins. The organizations claim that combining the NMR-derived 3-dimensional atomic ...
Bruker and Lawrence...
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11-10-2011 08:09 PM
[NMR paper] Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically l
Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies.
Related Articles Intein-based biosynthetic incorporation of unlabeled protein tags into isotopically labeled proteins for NMR studies.
Nat Biotechnol. 2005 Jun;23(6):736-40
Authors: Züger S, Iwai H
Segmental isotopic labeling of proteins using protein ligation is a recently established in vitro method for incorporating isotopes into one domain or region of a protein to reduce the complexity of NMR spectra, thereby facilitating...
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11-25-2010 08:21 PM
[NMR paper] High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Applicati
High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy.
Related Articles High-level bacterial expression and 15N-alanine-labeling of bovine trypsin. Application to the study of trypsin-inhibitor complexes and trypsinogen activation by NMR spectroscopy.
Biochemistry. 2001 May 29;40(21):6275-83
Authors: Peterson FC, Gordon NC, Gettins PG
We describe here the high-level expression of bovine trypsinogen in E. coli, its...
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11-19-2010 08:32 PM
[NMR paper] A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation da
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
Related Articles A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
J Magn Reson. 1998 Feb;130(2):329-34
Authors: Daragan VA, Mayo KH
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational...
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11-17-2010 11:06 PM
[NMR software blog] Oh, Sugar
Oh, Sugar
I have good news! With a minimal simplification of my INADEQUATE filter I have been able to rescue the last cross-peak of cholesterol. It had been rejected because too near to the diagonal. I changed the code saying: "if it's on the diagonal, it is bad; if it's just near, let's accept it". So it is possible to have the perfect INADEQUATE of cholesterol, with all the expected cross-peaks IN and everything else OUT.
Yesterday I received another INADEQUATE spectrum, this time of sucrose. The S/N is still high enough to make my filter unnecessary. If I play with the contour plot all...
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09-03-2010 04:16 PM
[NMR paper] Defining the precision with which a protein structure is determined by NMR. Applicati
Defining the precision with which a protein structure is determined by NMR. Application to motilin.
Related Articles Defining the precision with which a protein structure is determined by NMR. Application to motilin.
Biochemistry. 1993 Feb 16;32(6):1610-7
Authors: Shriver J, Edmondson S
A simple procedure is introduced for accurately defining the precision with which the Cartesian coordinates of any macromolecular structure are determined by nuclear Overhauser data. The method utilizes an ensemble of structures obtained from an array of...