A critical view on conservative mutations
By analysing the surface composition of a set of protein 3D structures, complemented with predicted surface compositional information for homologous proteins, we have found significant evidence for a layer composition of protein structures. In the innermost and outermost parts of proteins there is a...
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Veröffentlicht in: | Protein engineering 2001-06, Vol.14 (6), p.397-402 |
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creator | Jonson, Per Harald Petersen, Steffen B. |
description | By analysing the surface composition of a set of protein 3D structures, complemented with predicted surface compositional information for homologous proteins, we have found significant evidence for a layer composition of protein structures. In the innermost and outermost parts of proteins there is a net negative charge, while the middle has a net positive charge. In addition, our findings indicate that the concept of conservative mutation needs substantial revision, e.g. very different spatial preferences were found for glutamic acid and aspartic acid. The alanine screening often used in protein engineering projects involves the substitution of residues to alanine, based on the assumption that alanine is a `neutral' residue. However, alanine has a high negative correlation with all but the non-polar residues. We therefore propose the use of, for example, serine as a substitute for the residues that are negatively correlated with alanine. |
doi_str_mv | 10.1093/protein/14.6.397 |
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subjects | amino acid properties Amino Acid Sequence Aspartic Acid - chemistry Glutamic Acid - chemistry Ions Models, Molecular Mutation Protein Conformation protein engineering Sequence Homology, Amino Acid solvent accessibility Solvents - pharmacology spatial contacts Static Electricity structural preference |
title | A critical view on conservative mutations |
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