scholarly journals Small Molecules Bound to Unique Sites in the Target Protein Binding Cleft of Calcium-Bound S100B As Characterized by Nuclear Magnetic Resonance and X-ray Crystallography

Biochemistry ◽  
2009 ◽  
Vol 48 (26) ◽  
pp. 6202-6212 ◽  
Author(s):  
Thomas H. Charpentier ◽  
Paul T. Wilder ◽  
Melissa A. Liriano ◽  
Kristen M. Varney ◽  
Shijun Zhong ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Protein Binding ◽  
Small Molecules ◽  
Target Protein ◽  
X Ray ◽  
X Ray Crystallography ◽  
Binding Cleft ◽  
Nuclear Magnetic

The crystal structure of ethyl-Z-3-amino-2-benzoyl-2-butenoate and measurement of the barrier to E,Z-isomerization

1980 ◽  
Vol 58 (17) ◽  
pp. 1821-1828 ◽  
Author(s):  
Gary D. Fallon ◽  
Bryan M. Gatehouse ◽  
Allan Pring ◽  
Ian D. Rae ◽  
Josephine A. Weigold
Keyword(s):  
Crystal Structure ◽  
Nuclear Magnetic Resonance ◽  
Hydrogen Bond ◽  
Free Energy ◽  
Magnetic Resonance ◽  
Energy Of Activation ◽  
X Ray ◽  
X Ray Crystallography ◽  
Free Energy Of Activation ◽  
Nuclear Magnetic

Ethyl-3-amino-2-benzoyl-2-butenoate crystallizes from pentane as either the E (mp 82–84 °C) or the Z-isomer (mp 95.5–96.5 °C). The E isomer is less stable, and changes spontaneously into the Z, which bas been identified by X-ray crystallography. The structure is characterised by an N–H/ester CO hydrogen bond and a very long C2—C3 bond (1.39 Å). Nuclear magnetic resonance methods have been used to measure the rate of [Formula: see text] isomerization at several temperatures, leading to the estimate that the free energy of activation at 268 K is 56 ± 8 kJ.

Synthesis and conformation studies by x-ray crystallography and nuclear magnetic resonance of cyclo(L-Phe-L-Pro-D-Ala)2

1984 ◽  
Vol 106 (13) ◽  
pp. 3844-3850 ◽  
Author(s):  
Gopinath Kartha ◽  
K. Krishna Bhandary ◽  
Kenneth D. Kopple ◽  
Anita Go ◽  
Peng Peng Zhu
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
X Ray ◽  
X Ray Crystallography ◽  
Nuclear Magnetic

scholarly journals Unravelling Conformational Aspects of Milk Protein Structure—Contributions from Nuclear Magnetic Resonance Studies

Foods ◽  
2020 ◽  
Vol 9 (8) ◽  
pp. 1128
Author(s):  
Tatijana Markoska ◽  
Todor Vasiljevic ◽  
Thom Huppertz
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Calcium Phosphate ◽  
Dairy Products ◽  
Tertiary Structure ◽  
Whey Proteins ◽  
Milk Proteins ◽  
X Ray ◽  
X Ray Crystallography ◽  
Nuclear Magnetic

Changes in the molecular structure and association of milk proteins lead to many desirable (under controlled conditions) or undesirable characteristics of dairy products. Several methods have been used to study the structure of milk proteins and changes therein in different environments. Whey proteins are an excellent model for secondary structure studies using circular dichroism (CD), Fourier-transform infrared spectroscopy (FTIR) and tertiary structure studies using X-ray crystallography and nuclear magnetic resonance (NMR). However, caseins, the most abundant protein class in milk, are far more difficult to characterize. The tertiary structure of caseins cannot be observed by X-ray crystallography due to the inability to crystallize caseins. However, NMR is an appropriate approach for structural elucidation. Thus far, NMR was applied on specific peptides of individual caseins of the molecules including phosphoserine centers and colloidal calcium phosphate. The literature focuses on these parts of the molecule due to its importance in building the sub-unit particles involving individual caseins and calcium phosphate nanoclusters. This review focuses on present structural studies of milk proteins using NMR and their importance in dairy processing.

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