1flx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:11, 28 July 2021) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
{{Theoretical_model}}
{{Theoretical_model}}
-
{{Seed}}
 
-
[[Image:1flx.png|left|200px]]
 
-
<!--
+
==DE NOVO DESIGN, EXPRESSION, AND CHARACTERIZATION OF FELIX: A FOUR-HELIX BUNDLE PROTEIN OF NATIVE-LIKE SEQUENCE==
-
The line below this paragraph, containing "STRUCTURE_1flx", creates the "Structure Box" on the page.
+
<StructureSection load='1flx' size='340' side='right'caption='[[1flx]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<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>
-
or leave the SCENE parameter empty for the default display.
+
</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>
-
{{STRUCTURE_1flx| PDB=1flx | SCENE= }}
+
<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===
+
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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_2392678}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1flx" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 2392678 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_2392678}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Theoretical Model]]
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLX OCA].
+
[[Category: Large Structures]]
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:2392678</ref><references group="xtra"/>
+
[[Category: Quinn, T P]]
[[Category: Quinn, T P]]
[[Category: Richardson, D C]]
[[Category: Richardson, D C]]
[[Category: Richardson, J S]]
[[Category: Richardson, J S]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:47:06 2010''
 

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

PDB ID 1flx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools