کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5371641 | 1503958 | 2010 | 7 صفحه PDF | دانلود رایگان |

We explore the thermodynamic properties of three different fibrils of the peptide hormone glucagon, formed under different salt conditions (glycine, sulfate and NaCl, respectively), and differing considerably in compactness. The three fibrils display a large variation in the specific heat capacity ÎCp determined by isothermal titration calorimetry. Sulfate fibrils show a negative ÎCp expected from a folding reaction, while the ÎCp for glycine fibrils is essentially zero. NaCl fibrils, which are less stable than the other fibrils, have a large and positive âCp. The predicted change in solvent accessible area is not a useful predictor of fibrillar ÎCp unlike the case for globular proteins. We speculate that strong backbone interactions may lead to the unfavorable burial of polar side residues, water and/or charged groups which all can have major influence on the change in âCp. These results highlight differences in the driving forces of native folding and fibril formation.
Journal: Biophysical Chemistry - Volume 149, Issues 1â2, June 2010, Pages 40-46