Measuring the conformational stability of a protein
Description
<jats:title>Abstract</jats:title> <jats:p>The stability of proteins, especially enzymes, has long been a practical concern (1), because this is usually the factor that most limits their usefulness. There are two very different aspects of protein stability. One is the chemical stability of the covalent structure, which involves covalent changes and is usually irreversible. The other is the conformational stability of the folded state, in the absence of covalent changes (2-8). The latter is the subject of this chapter, which will describe the simplest methods available for measuring how much more stable is the folded conformation of a protein than its unfolded conformations.</jats:p>
Journal
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- Protein Structure
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Protein Structure 299-322, 1997-02-20
Oxford University PressOxford