Related ArticlesObserving 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 group of the Val-E11 resonates in a clear spectral region at -2.76 ppm and responds to dynamic changes in cellular oxygenation. With CO, the signal shifts to -2.4 ppm. The Val-E11 peak assignment and its response to oxygen and CO agree perfectly with previous myoglobin solution studies. Intracellular oxygen level can now be determined in vivo with the signal intensity ratio of oxymyoglobin/deoxymyoglobin, reflected by the Val-E11 and His-F8 peaks in the 1H NMR spectra. Moreover, protein structure-function relationship in vivo can now be probed.
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] Evaluation of parameters critical to observing proteins inside living Escherichia col
Evaluation of parameters critical to observing proteins inside living Escherichia coli by in-cell NMR spectroscopy.
Related Articles Evaluation 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...
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[NMR paper] H-NMR signal of Arenicola marina myoglobin in vivo as an index of tissue oxygenation.
H-NMR signal of Arenicola marina myoglobin in vivo as an index of tissue oxygenation.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles H-NMR signal of Arenicola marina myoglobin in vivo as an index of tissue oxygenation.
Eur J Biochem. 1996 Feb 1;235(3):622-8
Authors: Kreutzer U, Jue T
Key questions on how intertidal animals adapt to hypoxic stress center on the high energy phosphate response to decreasing oxygenation. With recent...
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[NMR paper] 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Es
1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Related Articles 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Biochemistry. 1991 Oct 15;30(41):10043-57
Authors: Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S
IIIGlc is an 18.1-kDa signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase...
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[NMR paper] 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Es
1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Related Articles 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Biochemistry. 1991 Oct 15;30(41):10043-57
Authors: Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S
IIIGlc is an 18.1-kDa signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase...
Observing the 1H NMR signal of the myoglobin Val-E11 in myocardium: an index of cellu
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