Mutational analysis of a protein-folding pathway
The effects of amino-acid replacements on the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor have been examined. Replacements at three sites destabilize the native protein relative to the unfolded state, but have different effects on the relative stabilities of the disulph...
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| Veröffentlicht in: | Nature (London) 1989-03, Vol.338 (6211), p.127-132 |
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| container_issue | 6211 |
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| container_title | Nature (London) |
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| creator | Goldenberg, David P Frieden, Richard W Haack, Julie A Morrison, Thomas B |
| description | The effects of amino-acid replacements on the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor have been examined. Replacements at three sites destabilize the native protein relative to the unfolded state, but have different effects on the relative stabilities of the disulphide-bonded folding intermediates, thus allowing the roles of the altered residues during folding to be distinguished. |
| doi_str_mv | 10.1038/338127a0 |
| format | Article |
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| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 1989-03, Vol.338 (6211), p.127-132 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78884519 |
| source | MEDLINE; Nature; Alma/SFX Local Collection |
| subjects | Acids Amino Acid Sequence Aprotinin Biological and medical sciences Biology cattle Conformational dynamics in molecular biology Fundamental and applied biological sciences. Psychology Kinetics Models, Molecular Molecular biophysics Mutation Protein Conformation |
| title | Mutational analysis of a protein-folding pathway |
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