Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit. Monitoring conformational changes due to substitutions at position 49

1990 ◽  
Vol 189 (3) ◽  
pp. 667-673 ◽  
Author(s):  
Shintaro SAWADA ◽  
Hideo AKUTSU ◽  
Kyoko OGASAHARA ◽  
Katsuhide YUTANI
Keyword(s):  
1H Nmr ◽  
Conformational Changes ◽  
Alpha Subunit ◽  
Tryptophan Synthase ◽  
Nmr Spectrum

scholarly journals Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Qing-Tao He ◽  
Peng Xiao ◽  
Shen-Ming Huang ◽  
Ying-Li Jia ◽  
Zhong-Liang Zhu ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Conformational Changes ◽  
Nmr Spectrum ◽  
H Nmr ◽  
Interaction Sites ◽  
Receptor Interactions ◽  
Remote Sites ◽  
Genetic Code Expansion ◽  
G Protein Coupled ◽  
Interaction Change

AbstractArrestins recognize different receptor phosphorylation patterns and convert this information to selective arrestin functions to expand the functional diversity of the G protein-coupled receptor (GPCR) superfamilies. However, the principles governing arrestin-phospho-receptor interactions, as well as the contribution of each single phospho-interaction to selective arrestin structural and functional states, are undefined. Here, we determined the crystal structures of arrestin2 in complex with four different phosphopeptides derived from the vasopressin receptor-2 (V2R) C-tail. A comparison of these four crystal structures with previously solved Arrestin2 structures demonstrated that a single phospho-interaction change results in measurable conformational changes at remote sites in the complex. This conformational bias introduced by specific phosphorylation patterns was further inspected by FRET and 1H NMR spectrum analysis facilitated via genetic code expansion. Moreover, an interdependent phospho-binding mechanism of phospho-receptor-arrestin interactions between different phospho-interaction sites was unexpectedly revealed. Taken together, our results provide evidence showing that phospho-interaction changes at different arrestin sites can elicit changes in affinity and structural states at remote sites, which correlate with selective arrestin functions.

Study on the Inclusion Behavior of Cucurbit [n] uril with Phenylalanine

2011 ◽  
Vol 197-198 ◽  
pp. 1153-1156
Author(s):  
Ning Chen ◽  
Ya Bin Li
Keyword(s):  
1H Nmr ◽  
Interaction Mechanism ◽  
Acetate Buffer Solution ◽  
Molar Ratio ◽  
High Concentration ◽  
Buffer Solution ◽  
Visible Absorption ◽  
Nmr Spectrum ◽  
Application Range ◽  
Uv Visible

The characteristics of host-guest complexes between cucurbit[n]uril (CB [n]) and phenylalanine were investigated by UV-visible absorption spectroscopy in acetate buffer solution at room temperature. It was found that the UV-visible absorption increased steadily with constantly dropping the high concentration of cucurbit[6]uril (CB [6]) and cucurbit[8]uril (CB [8]) in the phenylalanine solution which indicates that there are some interaction betweenCB [n] and phenylalanine.Then CB [6] and phenylalanine at molar ratio of 1:1 to weigh while CB [8] and phenylalanine at molar ratio of 1:2, respectively, are both demonstrated by 1H NMR spectra. 1H NMR spectrum of complexes was obtained, indicating an enthalpic driving force for host-guest complexes. The possible interaction mechanism and inclusion mode were also discussed. This work may extend the application range of CB [n] in supramolecular and pharmaceutical analysis.

Aluminum Fluoride Activation of Bovine Transducin Induces Two Distinct Conformational Changes in the .alpha. Subunit

Biochemistry ◽  
1994 ◽  
Vol 33 (33) ◽  
pp. 10178-10184 ◽  
Author(s):  
Rohit Mittal ◽  
Richard A. Cerione ◽  
Jon W. Erickson
Keyword(s):  
Conformational Changes ◽  
Alpha Subunit ◽  
Aluminum Fluoride

scholarly journals Identification of Methyl Resonances in the 1H NMR Spectrum of Incubated Blood Cell Lysates

1989 ◽  
Vol 264 (4) ◽  
pp. 2100-2107 ◽  
Author(s):  
G L Mendz ◽  
M N McCall ◽  
P W Kuchel
Keyword(s):  
Blood Cell ◽  
1H Nmr ◽  
Nmr Spectrum ◽  
Cell Lysates

Solving the 31P{1H} NMR spectrum of (Me3Si)3P7 as B[AC]3 case

2017 ◽  
Vol 192 (6) ◽  
pp. 727-731
Author(s):  
Eberhard Matern ◽  
Michael Engelhardt ◽  
Gerhard Hägele
Keyword(s):  
1H Nmr ◽  
Nmr Spectrum

scholarly journals One-Dimensional 13C NMR Is a Simple and Highly Quantitative Method for Enantiodiscrimination

Molecules ◽  
2018 ◽  
Vol 23 (7) ◽  
pp. 1785 ◽  
Author(s):  
Peter Lankhorst ◽  
Jozef van Rijn ◽  
Alexander Duchateau
Keyword(s):  
1H Nmr ◽  
13C Nmr ◽  
Quantitative Method ◽  
Enantiomeric Excess ◽  
Nmr Spectrum ◽  
One Dimensional ◽  
Nmr Method ◽  
Relative Standard ◽  
Excess Value ◽  
Chiral Solvating Agent

The discrimination of enantiomers of mandelonitrile by means of 1D 13C NMR and with the aid of the chiral solvating agent (S)-(+)-1-(9-anthryl)-2,2,2-trifluoroethanol (TFAE) is presented. 1H NMR fails for this specific compound because proton signals either overlap with the signals of the chiral solvating agent or do not show separation between the (S)-enantiomer and the (R)-enantiomer. The 13C NMR method is validated by preparing artificial mixtures of the (R)-enantiomer and the racemate, and it is shown that with only 4 mg of mandelonitrile a detection limit of the minor enantiomer of 0.5% is obtained, corresponding to an enantiomeric excess value of 99%. Furthermore, the method shows high linearity, and has a small relative standard deviation of only 0.3% for the minor enantiomer when the relative abundance of this enantiomer is 20%. Therefore, the 13C NMR method is highly suitable for quantitative enantiodiscrimination. It is discussed that 13C NMR is preferred over 1H NMR in many situations, not only in molecules with more than one chiral center, resulting in complex mixtures of many stereoisomers, but also in the case of molecules with overlapping multiplets in the 1H NMR spectrum, and in the case of molecules with many quaternary carbon atoms, and therefore less abundant protons.

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