Two-dimensional nuclear magnetic resonance structure determination module for introductory biochemistry: synthesis and structural characterization of lyso-glycerophospholipids

2013 ◽  
Vol 41 (2) ◽  
pp. 87-94
Author(s):  
Teresa A. Garrett ◽  
Rebecca L. Rose ◽  
Sidney M. Bell
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Structural Characterization ◽  
Structure Determination ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Two Dimensional ◽  
Nuclear Magnetic

scholarly journals Structural Characterization of Amadori Rearrangement Product of Glucosylated Nα-Acetyl-Lysine by Nuclear Magnetic Resonance Spectroscopy

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Chuanjiang Li ◽  
Hui Wang ◽  
Manuel Juárez ◽  
Eric Dongliang Ruan
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Maillard Reaction ◽  
Structural Characterization ◽  
Resonance Spectroscopy ◽  
H Nmr ◽  
Amadori Rearrangement ◽  
C Nmr ◽  
Nuclear Magnetic

Maillard reaction is a nonenzymatic reaction between reducing sugars and free amino acid moieties, which is known as one of the most important modifications in food science. It is essential to characterize the structure of Amadori rearrangement products (ARPs) formed in the early stage of Maillard reaction. In the present study, the Nα-acetyl-lysine-glucose model had been successfully set up to produce ARP, Nα-acetyl-lysine-glucose. After HPLC purification, ARP had been identified by ESI-MS with intense [M+H]+ ion at 351 m/z and the purity of ARP was confirmed to be over 90% by the relative intensity of [M+H]+ ion. Further structural characterization of the ARP was accomplished by using nuclear magnetic resonance (NMR) spectroscopy, including 1D 1H NMR and 13C NMR, the distortionless enhancement by polarization transfer (DEPT-135) and 2D 1H-1H and 13C-1H correlation spectroscopy (COSY) and 2D nuclear overhauser enhancement spectroscopy (NOESY). The complexity of 1D 1H NMR and 13C NMR was observed due to the presence of isomers in glucose moiety of ARP. However, DEPT-135 and 2D NMR techniques provided more structural information to assign the 1H and 13C resonances of ARP. 2D NOESY had successfully confirmed the glycosylated site between 10-N in Nα-acetyl-lysine and 7′-C in glucose.

Nuclear Magnetic Resonance Structure of a Prototype Lin12-Notch Repeat Module from Human Notch1†

Biochemistry ◽  
2003 ◽  
Vol 42 (23) ◽  
pp. 7061-7067 ◽  
Author(s):  
Didem Vardar ◽  
Christopher L. North ◽  
Cheryll Sanchez-Irizarry ◽  
Jon C. Aster ◽  
Stephen C. Blacklow
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Resonance Structure ◽  
Nuclear Magnetic Resonance Structure ◽  
Nuclear Magnetic

Structural Characterization of Ca2+-ATPase-Bound Phospholamban in Lipid Bilayers by Solid-State Nuclear Magnetic Resonance (NMR) Spectroscopy†,‡

Biochemistry ◽  
2008 ◽  
Vol 47 (15) ◽  
pp. 4369-4376 ◽  
Author(s):  
Karsten Seidel ◽  
Ovidiu C. Andronesi ◽  
Joachim Krebs ◽  
Christian Griesinger ◽  
Howard S. Young ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Solid State ◽  
Nmr Spectroscopy ◽  
Magnetic Resonance ◽  
Lipid Bilayers ◽  
Structural Characterization ◽  
Nuclear Magnetic
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