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Microcalorimetry and the Molecular Recognition of Peptides and Proteins

Alan Cooper and Katherine E. McAuley-Hecht
Philosophical Transactions: Physical Sciences and Engineering
Vol. 345, No. 1674, The Chemistry of Biological Molecular Recognition (Oct. 15, 1993), pp. 23-35
Published by: Royal Society
Stable URL: http://www.jstor.org/stable/54195
Page Count: 13
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Microcalorimetry and the Molecular Recognition of Peptides and Proteins
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Abstract

Isothermal titration (ITC) and differential scanning calorimetry (DSC) techniques are now routinely applicable to the study of non-covalent interactions in biomolecular recognition. Examples from our own current work on peptide antibiotic interactions and protein folding illustrate what may be achieved. ITC binding studies of vancomycin antibiotics with model peptides give information about the thermo-dynamics of group interactions, and also demonstrate possible complexities due to ligand-induced aggregation processes. The thermal stability of proteins in mixed aqueous solvents, studied by DSC, shows how the balance of forces responsible for folding stability may switch, without markedly perturbing the native structure. Separate experiments on the molecular recognition of unfolded polypeptide chains by cyclodextrins are consistent with simple binding of these cyclic polysaccharides to exposed aromatic groups on the thermally denatured protein.

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