Carbon-13 nuclear magnetic resonance studies of structure and function in thyrotropin-releasing factor. Determination of the tautomeric form of histidine and relation to biology activity

Biochemistry ◽  
1974 ◽  
Vol 13 (17) ◽  
pp. 3443-3448 ◽  
Author(s):  
Roxanne Deslauiers ◽  
W. H. McGregor ◽  
D. Sarantakis ◽  
Ian C. P. Smith
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Tautomeric Form ◽  
Structure And Function ◽  
Magnetic Resonance Studies ◽  
And Function ◽  
Nuclear Magnetic

Applications of 31P nuclear magnetic resonance to studies of protein structure and function

1983 ◽  
Vol 61 (4) ◽  
pp. 155-164 ◽  
Author(s):  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Alkaline Phosphatase ◽  
Protein Structure ◽  
Magnetic Resonance ◽  
Glycogen Phosphorylase ◽  
Structure And Function ◽  
Resonance Spectroscopy ◽  
Protein Structure And Function ◽  
And Function ◽  
Nuclear Magnetic

Selective illustrative applications of phosphorus-31 nuclear magnetic resonance spectroscopy to the study of protein structure and function are reviewed, including the enzymes alkaline phosphatase, myosin, actin, and glycogen phosphorylase.

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