Nuclear Magnetic Resonance Spectroscopy of Proteins: The Hydrogen Bonding of Water in Bovine Serum Albumin Solutions

Nature ◽  
1961 ◽  
Vol 192 (4800) ◽  
pp. 324-326 ◽  
Author(s):  
F. A. BOVEY
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Hydrogen Bonding ◽  
Magnetic Resonance ◽  
Bovine Serum Albumin ◽  
Magnetic Resonance Spectroscopy ◽  
Serum Albumin ◽  
Nuclear Magnetic Resonance Spectroscopy ◽  
Bovine Serum ◽  
Resonance Spectroscopy ◽  
Nuclear Magnetic

HYDROGEN BONDING IN PHENOL, ANILINE, AND THIOPHENOL BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY AND CRYOSCOPY

1962 ◽  
Vol 40 (5) ◽  
pp. 963-965 ◽  
Author(s):  
B. D. Nageswara Rao ◽  
Putcha Venkateswarlu ◽  
A. S. N. Murthy ◽  
C. N. R. Rao
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Hydrogen Bonding ◽  
Magnetic Resonance ◽  
Magnetic Resonance Spectroscopy ◽  
Nuclear Magnetic Resonance Spectroscopy ◽  
Resonance Spectroscopy ◽  
Nuclear Magnetic

Hydrogen bonding in phenol, aniline, and thiophenol has been investigated by n.m.r. spectroscopy and cryoscopy. While phenol shows evidence for the presence of monomer–dimmer–polymer equilibrium, thiophenol only indicates low monomer–dimer equilibrium. The extent of association in these three systems decreases in the order phenol, aniline, thiophenol.

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