On the basis of studies of Asn to Ala mutants, the gain in stability from burying amide groups th... more On the basis of studies of Asn to Ala mutants, the gain in stability from burying amide groups that are hydrogen bonded to peptide groups is 80 cal/(mol A(3)). On the basis of similar studies of Leu to Ala and Ile to Val mutants, the gain in stability from burying -CH(2)- groups is 50 cal/(mol A(3)). Thus, the burial of an amide group contributes more to protein stability than the burial of an equivalent volume of -CH(2)- groups. Applying these results to folded proteins leads to the surprising conclusion that peptide group burial makes a larger contribution to protein stability than nonpolar side chain burial. Several studies have shown that the desolvation penalty for burying peptide groups is considerably smaller than generally thought. This suggests that the hydrogen bonding and van der Waals interactions of peptide groups in the tightly packed interior of folded protein are more favorable than similar interactions with water in the unfolded protein.
Angewandte Chemie International Edition in English, 1991
Proteins carry out the most important and difficult tasks in all living organisms. To do so, they... more Proteins carry out the most important and difficult tasks in all living organisms. To do so, they must often interact specifically with other small and large molecules. This requires that they fold to a globular conformation with a unique active site that is used for the specific interaction. Consequently, protein folding can be regarded as the “secret of life”. Biochemists and chemists have a great interest in elucidating the mechanism by which proteins fold and in predicting the folded conformation and its stability given just the amino acid sequence. This challenge is sometimes called the “protein folding problem”. The ability to construct proteins differing in sequence by one or more amino acids and to analyze their three‐dimensional structures by X‐ray crystallography and NMR spectroscopy is a powerful tool for investigating the conformational stability and folding of proteins. Several proteins are now under intensive study by this approach. One of these is ribonuclease T1.
On the basis of studies of Asn to Ala mutants, the gain in stability from burying amide groups th... more On the basis of studies of Asn to Ala mutants, the gain in stability from burying amide groups that are hydrogen bonded to peptide groups is 80 cal/(mol A(3)). On the basis of similar studies of Leu to Ala and Ile to Val mutants, the gain in stability from burying -CH(2)- groups is 50 cal/(mol A(3)). Thus, the burial of an amide group contributes more to protein stability than the burial of an equivalent volume of -CH(2)- groups. Applying these results to folded proteins leads to the surprising conclusion that peptide group burial makes a larger contribution to protein stability than nonpolar side chain burial. Several studies have shown that the desolvation penalty for burying peptide groups is considerably smaller than generally thought. This suggests that the hydrogen bonding and van der Waals interactions of peptide groups in the tightly packed interior of folded protein are more favorable than similar interactions with water in the unfolded protein.
Angewandte Chemie International Edition in English, 1991
Proteins carry out the most important and difficult tasks in all living organisms. To do so, they... more Proteins carry out the most important and difficult tasks in all living organisms. To do so, they must often interact specifically with other small and large molecules. This requires that they fold to a globular conformation with a unique active site that is used for the specific interaction. Consequently, protein folding can be regarded as the “secret of life”. Biochemists and chemists have a great interest in elucidating the mechanism by which proteins fold and in predicting the folded conformation and its stability given just the amino acid sequence. This challenge is sometimes called the “protein folding problem”. The ability to construct proteins differing in sequence by one or more amino acids and to analyze their three‐dimensional structures by X‐ray crystallography and NMR spectroscopy is a powerful tool for investigating the conformational stability and folding of proteins. Several proteins are now under intensive study by this approach. One of these is ribonuclease T1.
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