Related ArticlesEvaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.
J Am Chem Soc. 2001 Sep 19;123(37):8895-901
Authors: Serber Z, Ledwidge R, Miller SM, Dötsch V
Our recently developed in-cell NMR procedure now enables one to observe protein conformations inside living cells. Optimization of the technique demonstrates that distinguishing the signals produced by a single protein species depends critically on protein overexpression levels and the correlation time in the cytoplasm. Less relevant is the selective incorporation of (15)N. Poorly expressed proteins, insoluble proteins, and proteins that cannot tumble freely due to associations within the cell cannot yet be observed. We show in-cell NMR spectra of bacterial NmerA and human calmodulin and discuss limitations of the technique as well as prospects for future applications.
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy
Abstract NMR spectroscopy has distinct advantages for providing insight into protein structures, but faces significant resolution challenges as protein size increases. To alleviate such resonance overlap issues, the ability to produce segmentally labeled proteins is beneficial. Here we show that the S. aureus transpeptidase sortase A can be used to catalyze the ligation of two separately expressed domains of the same protein, MecA (B. subtilis). The yield of purified, segmentally...
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Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
Observing selected domains in multi-domain proteins via sortase-mediated ligation and NMR spectroscopy.
J Biomol NMR. 2010 Dec 29;
Authors: Refaei MA, Combs A, Kojetin DJ, Cavanagh J, Caperelli C, Rance M, Sapitro J, Tsang P
NMR spectroscopy has distinct advantages for providing insight into protein structures, but faces significant resolution challenges as protein size increases. To alleviate such resonance overlap issues, the ability to...
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[NMR paper] An evaluation of detergents for NMR structural studies of membrane proteins.
An evaluation of detergents for NMR structural studies of membrane proteins.
Related Articles An evaluation of detergents for NMR structural studies of membrane proteins.
J Biomol NMR. 2004 Jan;28(1):43-57
Authors: Krueger-Koplin RD, Sorgen PL, Krueger-Koplin ST, Rivera-Torres IO, Cahill SM, Hicks DB, Grinius L, Krulwich TA, Girvin ME
Structural information on membrane proteins lags far behind that on soluble proteins, in large part due to difficulties producing homogeneous, stable, structurally relevant samples in a membrane-like environment....
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[NMR paper] Contact model for the prediction of NMR N-H order parameters in globular proteins.
Contact model for the prediction of NMR N-H order parameters in globular proteins.
Related Articles Contact model for the prediction of NMR N-H order parameters in globular proteins.
J Am Chem Soc. 2002 Oct 30;124(43):12654-5
Authors: Zhang F, Brüschweiler R
An analytical relationship is presented for the estimation of NMR S2 order parameters of N-HN vectors of the protein backbone from high-resolution protein structures. The relationship solely depends on close contacts of the peptide plane to the rest of the protein. Application of the...
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[NMR paper] Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellu
Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellular oxygenation.
Proc Natl Acad Sci U S A. 1992 May 15;89(10):4731-3
Authors: Kreutzer U, Wang DS, Jue T
The 1H NMR signal from oxymyoglobin, a low-concentration diamagnetic protein, is visible in myocardial tissue. The methyl...
Evaluation of parameters critical to observing proteins inside living Escherichia col
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