Multi-State Proteins: Approach Allowing Experimental Determination of the Formation Order of Structure Elements in the Green Fluorescent Protein
| Autor: | Anatoly S. Glukhov, Tatiana V Povarnitsyna, Bogdan S. Melnik, Tatiana N. Melnik |
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| Rok vydání: | 2012 |
| Předmět: |
Proteomics
Models Molecular Protein Structure Protein Folding Protein Conformation Green Fluorescent Proteins Protein design Biophysics lcsh:Medicine Phi value analysis Protein Engineering Biochemistry Protein Chemistry Protein Structure Secondary Protein structure Lattice protein lcsh:Science Biology Protein secondary structure Multidisciplinary Chemistry Physics lcsh:R Proteins Protein structure prediction Protein tertiary structure Mutation lcsh:Q Protein folding Research Article |
| Zdroj: | PLoS ONE, Vol 7, Iss 11, p e48604 (2012) PLoS ONE |
| ISSN: | 1932-6203 |
| Popis: | The most complex problem in studying multi-state protein folding is the determination of the sequence of formation of protein intermediate states. A far more complex issue is to determine at what stages of protein folding its various parts (secondary structure elements) develop. The structure and properties of different intermediate states depend in particular on these parts. An experimental approach, named μ-analysis, which allows understanding the order of formation of structural elements upon folding of a multi-state protein was used in this study. In this approach the same elements of the protein secondary structure are "tested" by substitutions of single hydrophobic amino acids and by incorporation of cysteine bridges. Single substitutions of hydrophobic amino acids contribute to yielding information on the late stages of protein folding while incorporation of ss-bridges allows obtaining data on the initial stages of folding. As a result of such an μ-analysis, we have determined the order of formation of beta-hairpins upon folding of the green fluorescent protein. |
| Databáze: | OpenAIRE |
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