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Reduced BPTI is collapsed. A pulsed field gradient NMR study of unfolded and partially folded bovine pancreatic trypsin inhibitor by Hong Pan; George Barany; Clare Woodward is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract Pulsed field gradient NMR was used to measure the hydrodynamic behavior of unfolded variants of bovine pancreatic trypsin inhibitor (BPTI). The unfolded BPTI species studied were [R]~Abu~, at pH 4.5 and pH 2.5, and unfolded [14‐38]~Abu~ at pH 2.5. These were prepared by chemical synthesis. [R]~Abu~ is a model for reduced BPTI; all cysteine residues are replaced by α‐amino‐__n__‐butyric acid (Abu). [14‐38]~Abu~ retains cysteines 14 and 38, which form a disulfide bond, while the other cysteine residues are replaced by Abu. In the PFG experiments, the diffusion coefficient is measured as a function of protein concentration, and the value of __D__°—the diffusion coefficient extrapolated to infinite dilution—is determined. From D°, a value of the hydrodynamic radius, __R~h~__, is computed from the Stokes‐Einstein relationship. At pH 4.5, [R]~Abu~ has an __R__~h~ value significantly less than the value calculated for a random coil, while at pH 2.5 the experimental __R~h~__ value is the same as for a random coil. In view of the changes in NMR‐detected structure of [__R__]~Abu~ at pH 4.5 versus pH 2.5 (Pan H, Barbar E, Barany G, Woodward C. 1995. Extensive non‐random structure

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Author

Hong Pan; George Barany; Clare Woodward

Publisher

Cold Spring Harbor Laboratory Press; Wiley (John Wiley & Sons); Wiley-Blackwell; Wiley (ISSN 0961-8368)

Published

1997

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)