1flx
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
{{Theoretical_model}} | {{Theoretical_model}} | ||
| - | [[ | + | ==DE NOVO DESIGN, EXPRESSION, AND CHARACTERIZATION OF FELIX: A FOUR-HELIX BUNDLE PROTEIN OF NATIVE-LIKE SEQUENCE== |
| + | <StructureSection load='1flx' size='340' side='right'caption='[[1flx]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLX FirstGlance]. <br> | ||
| + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1flx FirstGlance], [https://www.ebi.ac.uk/pdbsum/1flx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1flx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The protein Felix was designed de novo to fold into an antiparallel four-helix bundle of specific topology. Its sequence of 79 amino acid residues is not homologous to any known protein sequence, but is "native-like" in that it is nonrepetitive and contains 19 of the 20 naturally occurring amino acids. Felix has been expressed from a synthetic gene cloned in Escherichia coli, and the protein has been purified to homogeneity. Physical characterization of the purified protein indicates that Felix (i) is monomeric in solution, (ii) is predominantly alpha-helical, (iii) contains a designed intramolecular disulfide bond linking the first and fourth helices, and (iv) buries its single tryptophan in an apolar environment and probably in close proximity with the disulfide bond. These physical properties rule out several alternative structures and indicate that Felix indeed folds into approximately the designed three-dimensional structure. | ||
| - | + | De novo design, expression, and characterization of Felix: a four-helix bundle protein of native-like sequence.,Hecht MH, Richardson JS, Richardson DC, Ogden RC Science. 1990 Aug 24;249(4971):884-91. PMID:2392678<ref>PMID:2392678</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1flx" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Theoretical Model]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Quinn, T P]] | [[Category: Quinn, T P]] | ||
[[Category: Richardson, D C]] | [[Category: Richardson, D C]] | ||
[[Category: Richardson, J S]] | [[Category: Richardson, J S]] | ||
Current revision
| Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution. |
DE NOVO DESIGN, EXPRESSION, AND CHARACTERIZATION OF FELIX: A FOUR-HELIX BUNDLE PROTEIN OF NATIVE-LIKE SEQUENCE
| |||||||||||
