Protein Structure in the Lyophilized State: A Hydrogen Isotope Exchange/NMR Study with Bovine Pancreatic Trypsin Inhibitor

1994 ◽  
Vol 116 (21) ◽  
pp. 9420-9422 ◽  
Author(s):  
Umesh R. Desai ◽  
John J. Osterhout ◽  
Alexander M. Klibanov
Biochemistry ◽  
1997 ◽  
Vol 36 (11) ◽  
pp. 3383-3388 ◽  
Author(s):  
Elena Ilyina ◽  
Vikram Roongta ◽  
Hong Pan ◽  
Clare Woodward ◽  
Kevin H. Mayo

2018 ◽  
Vol 9 (21) ◽  
pp. 4814-4820 ◽  
Author(s):  
Reem Mousa ◽  
Shifra Lansky ◽  
Gil Shoham ◽  
Norman Metanis

The folding mechanism of the model protein bovine pancreatic trypsin inhibitor was revisited. By switching the solvent exposed disulfide bond with methylene thioacetal we uncovered a hidden pathway in its folding mechanism. In addition, this moiety enhanced protein stability while fully maintaining the protein structure and biological function.


Author(s):  
Daria S. Timofeeva ◽  
David M Lindsay ◽  
W. J. Kerr ◽  
David James Nelson

Herein we examine the relationship between reaction rate and reaction selectivity in iridium-catalysed hydrogen isotope exchange (HIE) reactions directed by Lewis basic functional groups. We have recently develped a directing...


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