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• W2070933765 abstract "Amide hydrogen-deuterium exchange rates were measured in the PDZ2 domain from human phosphatase hPTP1E by 1 H- 15 N heteronuclear NMR spectroscopy. Protection factors were calculated for the slowly exchanging hydrogens in both the free PDZ2 domain and its complex with an octapeptide peptide, R-N-E-I-Q-S-L-V, derived from the C-terminus of the Fas receptor. Aside from a short α-helical region α1 (amino acids A-45 to D-49), the pattern of highly protected amides correlated well with the presence of hydrogen bonds in elements of the secondary structure. Hydrogen-bonded amides showed relatively fast exchange rates with half-lives of less than 9 h at pD 7.6 and 8°C. Protection factors, calculated as the ratio of theoretical (denatured) and observed exchange rates, showed less dispersion in maximal values than did the actual exchange rates. This behavior and the large pH dependence of the exchange rates suggest that amide exchange is close to the EX 2 limit. In this limit, exchange of the most protected amides occurs through a global unfolding mechanism. The free energy of the unfolding calculated from the largest protection factors is 4.8 ± 0.4 kcal/mol (1 cal = 4.184 J). This ΔG° closely matches the value measured by experiments with guanidine hydrochloride and fluorescence emission spectroscopy. Peptide binding to PDZ2 resulted in mostly global effects and stabilized the folded domain by 1.4 kcal/mol.Key words: PDZ2 from hPTP1E, amide exchange, ligand binding, NMR." @default.
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• W2070933765 date "1998-05-01" @default.
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• W2070933765 title "Effect of peptide binding on amide proton exchange rates in the PDZ2 domain from human phosphatase hPTP1E" @default.
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• W2070933765 doi "https://doi.org/10.1139/o98-069" @default.
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