Secondary Structure and Protein Deamidation
The deamidation reactions of asparagine residues in α‐helical and β‐turn secondary structural environments of peptides and proteins are reviewed. Both kinds of secondary structure tend to stabilize asparagine residues against deamidation, although the effects are not large. The effect of β‐sheet str...
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| Veröffentlicht in: | Journal of pharmaceutical sciences 1999-01, Vol.88 (1), p.8-13 |
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| container_title | Journal of pharmaceutical sciences |
| container_volume | 88 |
| creator | Xie, Minli Schowen, Richard L. |
| description | The deamidation reactions of asparagine residues in α‐helical and β‐turn secondary structural environments of peptides and proteins are reviewed. Both kinds of secondary structure tend to stabilize asparagine residues against deamidation, although the effects are not large. The effect of β‐sheet structures on asparagine stability is unclear, although simple considerations suggest a stabilization in this environment also. |
| doi_str_mv | 10.1021/js9802493 |
| format | Article |
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| ispartof | Journal of pharmaceutical sciences, 1999-01, Vol.88 (1), p.8-13 |
| issn | 0022-3549 1520-6017 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library; Alma/SFX Local Collection |
| subjects | Amides - metabolism Aminoacids, peptides. Hormones. Neuropeptides Analytical, structural and metabolic biochemistry Animals Asparagine - chemistry Asparagine - metabolism Biological and medical sciences Fundamental and applied biological sciences. Psychology Humans Protein Structure, Secondary Proteins Proteins - chemistry Proteins - metabolism |
| title | Secondary Structure and Protein Deamidation |
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