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Search Publications by: John P. Marino (Fed)

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Displaying 76 - 100 of 152

2D 1HN, 15N Correlated NMR Methods at Natural Abundance for Obtaining Structural Maps and Statistical Comparability of Monoclonal Antibodies

March 1, 2015
Author(s)
Luke Arbogast, Robert G. Brinson, Catherine A. Mouchahoir, James T. Hoopes, John Marino
Purpose High-resolution nuclear magnetic resonance spectroscopy (NMR) provides a robust approach for producing unique spectral signatures of protein higher order structure at atomic resolution. Such signatures can be used as a tool to establish consistency

Mapping Monoclonal Antibody Structure by 2D 13C NMR at Natural Abundance

March 1, 2015
Author(s)
Luke Arbogast, Robert G. Brinson, John Marino
Monoclonal antibodies (mAbs) represent an important and rapidly growing class of biotherapeutics. Correct folding of a mAb is critical for drug efficacy, while misfolding can impact safety by eliciting unwanted immune or other off-target responses. Robust

Probing the intracellular glutathione redox potential using in-cell NMR spectroscopy

January 2, 2014
Author(s)
Steve Y. Rhieu, Aaron A. Urbas, Daniel W. Bearden, John P. Marino, Vytautas Reipa, Katrice A. Lippa
Non-invasive and real-time analysis of cellular redox processes has been greatly hampered by lack of suitable measurement techniques. Here we describe an in-cell nuclear magnetic resonance (NMR)-based method for measuring the intracellular glutathione

Formation of dAMP-glycerol and dAMP-Tris derivatives by the Thermococcus kodakaraensis DNA primase

May 11, 2012
Author(s)
Zvi Kelman, John P. Marino, Jerard Hurwitz, Wiebke Chemnitz Galal, Miao Pan, Gary Giulian, Wei Yuan, Shuwei Li
In the presence of dATP, glycerol and Tris buffer, the DNA primase isolated from Thermococcus kodakaraensis (Tk) catalyzed the formation of two products that were identified as dAMP-glycerol and dAMP-Tris. These products were formed by the Tk p41 catalytic

NMR Analysis of Rhodopsin-Transducin Interactions

December 1, 2006
Author(s)
Kevin Ridge, John Marino, T Ngo, Eva Ramon, D M. Brabazon, N G. Abdulaev
Heterotrimeric G-protein activation by an agonist-stimulated G-protein coupled receptor (R*) requires the propagation of structural signals from the receptor interacting surfaces to the guanine nucleotide-binding pocket. Employing high-resolution NMR

Conformational Changes Associated With Receptor-Stimulated Guanine Nucleotide Exchange in a Heterotrimeric G-Protein a-Subunit: NMR Analysis of the GTPgS-Bound States

March 17, 2006
Author(s)
K D. Ridge, N G. Abdulaev, Xi-Cheng Zhang, T Ngo, D M. Brabazon, John P. Marino
Solution NMR studies of a 15N-labeled G-protein ?-subunit (G?) chimera (15N-ChiT) reconstituted heterotrimer have previously shown that binding of ??-subunits induces a pre-activated conformation in G? that may facilitate interaction with R* and guanine