Calculated Vertical Ionization Energies of the Common α-Amino Acids in the Gas Phase and in Solution

2011 ◽  
Vol 115 (13) ◽  
pp. 2900-2912 ◽  
Author(s):  
David M. Close
2004 ◽  
Vol 126 (6) ◽  
pp. 1836-1842 ◽  
Author(s):  
Catherine Kapota ◽  
Joël Lemaire ◽  
Philippe Maître ◽  
Gilles Ohanessian

1999 ◽  
Vol 71 (19) ◽  
pp. 4427-4429 ◽  
Author(s):  
W. Andy Tao ◽  
Duxi Zhang ◽  
Feng Wang ◽  
Peter D. Thomas ◽  
R. Graham Cooks

Proteins ◽  
1987 ◽  
pp. 383-394
Author(s):  
J. E. Shively ◽  
D. Hawke ◽  
R. M. Kutny ◽  
B. Krieger ◽  
J. L. Glajch

2009 ◽  
Vol 20 (11) ◽  
pp. 2116-2123 ◽  
Author(s):  
Scott Gronert ◽  
David C. Simpson ◽  
Keyanna M. Conner

Author(s):  
Sumukh Deshpande ◽  
Saikat Kumar Basu ◽  
Pooja Purohit

We have surveyed polypeptides with the optimal conformations of nests which are the common anion-binding motifs comprising 8% of the amino acids which are characterized by a structural depression or a hole. Using automated bioinformatics algorithm, novel ring structure of the nest has been found. Using automated algorithm, models of polypeptides were made in-silico (computationally) and oxygen atoms are inserted along the extension of the NH groups. These sophisticated algorithms allow insertion of atoms along the NH group at the correct distance which causes extension of the group thus forming hydrogen bond. Optimal conformations of these structures are found from these customized models. This study chapter provides a demonstration of an important discovery of optimum conformations of RL and LR nests by the use of sophisticated bioinformatics automation pipeline and a unique application of automation and control in bioinformatics.


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