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Raman study of the thermal behaviour and conformational stability of basic pancreatic trypsin inhibitor

✍ Scribed by Pedro Carmona; Marina Molina; Arantxa Rodríguez-Casado

Publisher
Springer
Year
2003
Tongue
English
Weight
297 KB
Volume
32
Category
Article
ISSN
1432-1017

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Structural stability of disulfide mutant
Structural stability of disulfide mutants of basic pancreatic trypsin inhibitor: A molecular dynamics study
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The structure and folding of basic pancreatic trypsin inhibitor (BPTI) has been studied extensively by experimental means. We report a computer simulation study of the structural stability of various disulfide mutants of BPTI, involving eight 250-psec molecular dynamics simulations of the proteins i

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## Abstract The longitudinal ^13^C spin relaxation times T~1~ and the ^13^C{^1^H} nuclear Overhauser enhancement were measured in a concentrated aqueous solution of the basic pancreatic trypsin inhibitor. The correlation time for overall rotational motions of the basic pancreatic trypsin inhibitor

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Collision cross sections have been measured for gas phase ions of native oxidized bovine pancreatic trypsin inhibitor (BPTI), native reduced BPTI and a mutant form of BPTI containing a single disulphide bond between residues 5 and 55 ([5-55] Ala BPTI). Cross sections for [5-55] Ala BPTI and reduced

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## Abstract Values of the association equilibrium constant (__K__~a~) for the binding of the native and of the cyanogen bromide‐cleaved bovine basic pancreatic trypsin inhibitor (native BPTI and [Hse lactone‐52]‐52,53‐__seco__‐BPTI, respectively) to neuraminidase‐treated porcine pancreatic β‐Kallik