Role of Backbone Solvation in Determining Thermodynamic β Propensities of the Amino Acids
There is a paradox concerning the β propensities of the amino acids: the amino acids with the highest β propensities such as valine and isoleucine have the highest tendency to desolvate the peptide backbone, which should result in a loss of stability. Nevertheless, backbone solvation, calculated as...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2002-02, Vol.99 (3), p.1309-1313 |
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| description | There is a paradox concerning the β propensities of the amino acids: the amino acids with the highest β propensities such as valine and isoleucine have the highest tendency to desolvate the peptide backbone, which should result in a loss of stability. Nevertheless, backbone solvation, calculated as electrostatic solvation free energy (ESF), is highly correlated with mutant stability in the zinc-finger system studied by Kim and Berg [Kim, C. A. & Berg, J. M. (1993) Nature (London) 362, 267-270], and valine and isoleucine are among the most stabilizing amino acids. This inverse correlation between stability and ESF can be explained, because the mutant ESF differences in the unfolded protein are larger than in the native protein. Consequently, mutations such as Ala to Val destabilize the unfolded form more than the native protein. By comparing mutant ΔESF values in isolated β-strands versus β-sheets, we conclude that amino acids with high β propensities should exert their stabilizing effects at early stages in folding. This deduction agrees with the studies by Clarke and coworkers [Lorch, M., Mason, J. M., Clarke, A. R. & Parker, M. J. (1999) Biochemistry 38, 1377-1385, and Lorch, M., Mason, J. M., Sessions, R. B. & Clarke, A. R. (2000) Biochemistry 39, 3480-3485] of the thermodynamics of folding of the β-sheet protein CD2.d1. |
| doi_str_mv | 10.1073/pnas.032665499 |
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Nevertheless, backbone solvation, calculated as electrostatic solvation free energy (ESF), is highly correlated with mutant stability in the zinc-finger system studied by Kim and Berg [Kim, C. A. & Berg, J. M. (1993) Nature (London) 362, 267-270], and valine and isoleucine are among the most stabilizing amino acids. This inverse correlation between stability and ESF can be explained, because the mutant ESF differences in the unfolded protein are larger than in the native protein. Consequently, mutations such as Ala to Val destabilize the unfolded form more than the native protein. By comparing mutant ΔESF values in isolated β-strands versus β-sheets, we conclude that amino acids with high β propensities should exert their stabilizing effects at early stages in folding. This deduction agrees with the studies by Clarke and coworkers [Lorch, M., Mason, J. M., Clarke, A. R. & Parker, M. J. (1999) Biochemistry 38, 1377-1385, and Lorch, M., Mason, J. M., Sessions, R. B. & Clarke, A. R. 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| subjects | Amino Acid Sequence Amino acids Amino Acids - chemistry Biochemistry Biological Sciences Biophysics Correlation coefficients Correlations Drug Stability Electrostatics Enthalpy Free energy Isoleucine - chemistry Mutation Peptides - chemistry Protein Folding Protein Structure, Secondary Proteins Solubility Solvation Solvents Static Electricity Thermodynamics Valine - chemistry |
| title | Role of Backbone Solvation in Determining Thermodynamic β Propensities of the Amino Acids |
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