Abstract
Proteins are characterized by a marginal stability of their secondary and tertiary structure that renders them susceptible to stability perturbations by single amino acid exchanges. One of the most powerful techniques to determine the typical thermodynamic stability parameters is high sensitivity scanning microcalorimetry. The present paper describes some basic methodological aspects of the technique. Main attention is, however, focussed on the determination and magnitude of covalent and noncovalent contributions to overall protein stability. Two well defined proteins, bovine pancreatic trypsin inhibitor /BPTI/ and /ROP/ have served to exemplify the general rationale of the approach.
Published Version
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