The gauche effect is governed by internal hydrogen bond in 2-amino-2-methyl-propanol

2014 ◽  
Vol 1072 ◽  
pp. 203-207 ◽  
Author(s):  
Laize A.F. Andrade ◽  
Josué M. Silla ◽  
Matheus P. Freitas
Keyword(s):  
Hydrogen Bond ◽  
Gauche Effect ◽  
Internal Hydrogen ◽  
Internal Hydrogen Bond

Internal Hydrogen Bond Formation in a syn-Hydroxyepoxide

Science ◽  
1982 ◽  
Vol 215 (4533) ◽  
pp. 695-696 ◽  
Author(s):  
J. P. GLUSKER ◽  
D. E. ZACHARIAS ◽  
D. L. WHALEN ◽  
S. FRIEDMAN ◽  
T. M. POHL
Keyword(s):  
Hydrogen Bond ◽  
Bond Formation ◽  
Hydrogen Bond Formation ◽  
Internal Hydrogen ◽  
Internal Hydrogen Bond

A Single α-Helical Turn Stabilized by Replacement of an Internal Hydrogen Bond with a Covalent Ethylene Bridge

2009 ◽  
Vol 121 (31) ◽  
pp. 5785-5788 ◽  
Author(s):  
Andrea J. Vernall ◽  
Peter Cassidy ◽  
Paul F. Alewood
Keyword(s):  
Hydrogen Bond ◽  
Ethylene Bridge ◽  
Internal Hydrogen ◽  
Internal Hydrogen Bond ◽  
Helical Turn

scholarly journals Increasing the thermostability of the neutral proteinase of Bacillus stearothermophilus by improvement of internal hydrogen-bonding

1992 ◽  
Vol 285 (2) ◽  
pp. 625-628 ◽  
Author(s):  
V G Eijsink ◽  
G Vriend ◽  
J R Van der Zee ◽  
B Van den Burg ◽  
G Venema
Keyword(s):  
Molecular Dynamics ◽  
Hydrogen Bond ◽  
Bacillus Stearothermophilus ◽  
Site Directed Mutagenesis ◽  
Internal Cavity ◽  
Directed Mutagenesis ◽  
Neutral Proteinase ◽  
Internal Hydrogen ◽  
Internal Hydrogen Bond ◽  
Dynamics Simulations

In an attempt to increase the thermostability of the neutral proteinase of Bacillus stearothermophilus the buried Ala-170 was replaced by serine. Molecular-dynamics simulations showed that Ser-170 stabilizes the enzyme by formation of an internal hydrogen bond. In addition, the hydroxy group of Ser-170 could contribute to stability by filling an internal cavity. After the introduction of the mutation, using site-directed-mutagenesis techniques, an increase in stability of 0.7 +/- 0.1 degrees C was obtained.

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