Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution

Radzicka, Anna; Wolfenden, Richard

doi:10.1021/bi00405a042

Cited by 591 publications

(641 citation statements)

References 30 publications

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“…In this case the difference in hydrophobicity might offer an explc, nation, since the indole side chain of tryptophan is more hydropbobic than the phenol group of tyrosine. The difference in free energy change upon transferring these side chains from water to cyclohexane has been measured to be 10.32 kJ/mol, which gives an estimate of the magnitude of their difference in hydrophobicity [16]. Other plausible explanations can be, for example, the difference in charge-transfer properties between the phenol and the indole aromatic systems.…”

Section: Resultsmentioning

confidence: 99%

The difference in affinity between two fungal cellulose‐binding domains is dominated by a single amino acid substitution

et al. 1995

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Cellulose-binding domains (CBDs) form distinct functional units of most cellulolytic enzymes. We have compared the cellulose-binding affinities of the CBDs of ceilobiohydrolase 1 (CBHI) and endoglucanase I (EGI) from the fungus Trichoderma reeseL The CBD of EGI had significantly higher affinity than that of CBHI. Four variants of the CBHI CBD were made in order to identify the residues responsible for the increased affinity in EGI. Most of the difference could be ascribed to a replacement of a tyrosine by a tryptophan on the flat cellulose-binding face.

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Section: Resultsmentioning

confidence: 99%

The difference in affinity between two fungal cellulose‐binding domains is dominated by a single amino acid substitution

et al. 1995

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“…If the cyclohexane-to-water transfer data of Radzicka and Wolfenden (1988) were used, the minimum values (the lower ends of the boxes in Fig. 2) would be higher.…”

Section: Discussionmentioning

confidence: 99%

Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size

Lee

1993

Protein Science

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Although the hydrophobic effect is generally considered to be one of the most important forces in stabilizing the folded structure of a globular protein molecule, there is a lack of consensus on the precise magnitude of this effect. The magnitude of the hydrophobic effect is most directly measured by observing the change in stability of a protein molecule when a n internal hydrophobic residue is mutated to another of smaller size. Results of such measurements have, however, been confusing because they vary greatly and are generally considerably larger than expected from the transfer free energies of corresponding small molecules. In this article, a thermodynamic argument is presented to show (1) that the variation is mainly due to that in the flexibility of the protein molecule at the site of mutation, (2) that the maximum destabilization occurs when the protein at the site of mutation is rigid, in which case the value of the destabilization is approximately given by the work of cavity formation in water, and (3) that the transfer free energy approximately gives the minimum of the range of variations. The best numerical agreements between the small molecule and the protein systems are obtained when the data from the small molecule system are expressed as the molarity-based standard free energies without other corrections.

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“…They emphasize the effect of neighboring side chains (''occlusion'') in reducing the exposure of a given side chain to water. Radzicka and Wolfenden [16] studied a completely nonpolar solvent, cyclohexane, and observed that the transfer free energies of hydrocarbons are quite different when cyclohexane is the nonaqueous solvent as compared to n-octanol.…”

Section: Historymentioning

confidence: 99%

“…[16]). The model solutes undergoing transfer represent the amino acid side chains shown on the plot.…”

Section: Historymentioning

confidence: 99%

Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals Interactions, Peptide Hydrogen Bonds, and Peptide Solvation

Baldwin¹

2005

Protein Folding Handbook

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Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cyclohexane, 1-octanol, and neutral aqueous solution

Cited by 591 publications

References 30 publications

The difference in affinity between two fungal cellulose‐binding domains is dominated by a single amino acid substitution

The difference in affinity between two fungal cellulose‐binding domains is dominated by a single amino acid substitution

Estimation of the maximum change in stability of globular proteins upon mutation of a hydrophobic residue to another of smaller size

Weak Interactions in Protein Folding: Hydrophobic Free Energy, van der Waals Interactions, Peptide Hydrogen Bonds, and Peptide Solvation

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