| Title |
Synthetic Biology of Proteins: Tuning GFPs Folding and Stability with Fluoroproline
|
|---|---|
| Published in |
PLOS ONE, February 2008
|
| DOI | 10.1371/journal.pone.0001680 |
| Pubmed ID | |
| Authors |
Thomas Steiner, Petra Hess, Jae Hyun Bae, Birgit Wiltschi, Luis Moroder, Nediljko Budisa |
| Abstract |
Proline residues affect protein folding and stability via cis/trans isomerization of peptide bonds and by the C(gamma)-exo or -endo puckering of their pyrrolidine rings. Peptide bond conformation as well as puckering propensity can be manipulated by proper choice of ring substituents, e.g. C(gamma)-fluorination. Synthetic chemistry has routinely exploited ring-substituted proline analogs in order to change, modulate or control folding and stability of peptides. |
Mendeley readers
The data shown below were compiled from readership statistics for 136 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 6 | 4% |
| Germany | 2 | 1% |
| France | 1 | <1% |
| Portugal | 1 | <1% |
| Czechia | 1 | <1% |
| Brazil | 1 | <1% |
| Canada | 1 | <1% |
| United Kingdom | 1 | <1% |
| Unknown | 122 | 90% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 32 | 24% |
| Researcher | 27 | 20% |
| Student > Master | 16 | 12% |
| Student > Bachelor | 11 | 8% |
| Other | 10 | 7% |
| Other | 22 | 16% |
| Unknown | 18 | 13% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 60 | 44% |
| Biochemistry, Genetics and Molecular Biology | 23 | 17% |
| Chemistry | 20 | 15% |
| Social Sciences | 3 | 2% |
| Pharmacology, Toxicology and Pharmaceutical Science | 2 | 1% |
| Other | 8 | 6% |
| Unknown | 20 | 15% |