scholarly journals Ultra-high resolution structure of a new polymorphic form of bovine pancreatic trypsin inhibitor

2000 ◽  
Vol 56 (s1) ◽  
pp. s306-s306
Author(s):  
A. Addlagatta ◽  
H. Czapinska ◽  
Sz. Krzywda ◽  
J. Otlewski ◽  
M. Jaskólski
Keyword(s):  
High Resolution ◽  
Trypsin Inhibitor ◽  
Polymorphic Form ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Pancreatic Trypsin Inhibitor ◽  
High Resolution Structure ◽  
Resolution Structure

High-resolution structure of bovine pancreatic trypsin inhibitor with altered binding loop sequence

2000 ◽  
Vol 295 (5) ◽  
pp. 1237-1249 ◽  
Author(s):  
Honorata Czapinska ◽  
Jacek Otlewski ◽  
Szymon Krzywda ◽  
George M Sheldrick ◽  
Mariusz Jaskólski
Keyword(s):  
High Resolution ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Loop Sequence ◽  
Pancreatic Trypsin Inhibitor ◽  
High Resolution Structure ◽  
Binding Loop ◽  
Resolution Structure

The Study of Macromolecular Dynamics by High Resolution NMR

1980 ◽  
Vol 34 (3) ◽  
pp. 299-305 ◽  
Author(s):  
A. Ribeiro ◽  
N. G. Wade-Jardetzky ◽  
R. King ◽  
O. Jardetzky
Keyword(s):  
High Resolution ◽  
Trypsin Inhibitor ◽  
Bovine Pancreatic Trypsin Inhibitor ◽  
Relaxation Data ◽  
Relaxation Theory ◽  
Small Protein ◽  
High Resolution Nmr ◽  
Macromolecular Dynamics ◽  
Pancreatic Trypsin Inhibitor

The measurement and interpretation of relaxation data on macromolecules present special problems. The required instrumental conditions and extensions of relaxation theory are outlined and illustrated by the analysis of 13C and 1H relaxation data on a small protein (bovine pancreatic trypsin inhibitor).

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