| Autor: |
Henzl, Michael T., Wycoff, Wei G., Larson, John D., Likos, John J. |
| Zdroj: |
Protein Science: A Publication of the Protein Society; 2002, Vol. 11 Issue 1, p158-173, 16p |
| Abstrakt: |
15N relaxation data for Ca2+-bound rat β-parvalbumin (a.k.a. oncomodulin) were analyzed using the Lipari-Szabo formalism and compared with existing data for rat α-parvalbumin. Although the average S2 values for the two proteins are very similar (0.85 for α, 0.84 for β), residue-by-residue inspection reveals systematic differences. α tends to have the lower S2 value in helical regions; β tends to have the lower value in the loop regions. Rat β was also examined in the Ca2+-free state. The 59 assigned residues displayed an average order parameter (0.90) significantly greater than the corresponding residues in the Ca2+-loaded form. The pentacarboxylate variants of rat β-S55D and G98D-also were examined in the Ca2+-bound state. Although both mutations significantly heighten Ca2+ affinity, they utilize distinct energetic strategies. S55D improves the Ca2+-binding enthalpy; G98D improves the binding entropy. They also show disparate peptide backbone dynamics. Whereas β G98D displays an average order parameter (0.87) slightly greater than that of the wild-type protein, β S55D displays an average order parameter (0.82) slightly lower than wild-type β. Furthermore, whereas just two backbone N-H bonds in β G98D show internal motion on the 20-200-psec timescale, fully 52 of the 93 residues analyzed in β S55D show this behavior. These findings suggest that the increased electrostatic repulsion attendant to introduction of an additional carboxylate into the CD site ligand array impedes backbone vibrational motion throughout the molecule. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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