2fcq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2fcq.gif|left|200px]] | [[Image:2fcq.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_2fcq", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_2fcq| PDB=2fcq | SCENE= }} | |||
}} | |||
'''X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group''' | '''X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
2FCQ is a [[Single protein]] structure | 2FCQ is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCQ OCA]. | ||
==Reference== | ==Reference== | ||
| Line 30: | Line 27: | ||
[[Category: Makhatadze, G I.]] | [[Category: Makhatadze, G I.]] | ||
[[Category: Tereshko, V.]] | [[Category: Tereshko, V.]] | ||
[[Category: | [[Category: Ubiquitin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:44:31 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 03:44, 4 May 2008
X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group
OverviewOverview
The alpha-helix is a fundamental protein structural motif and is frequently terminated by a glycine residue. Explanations for the predominance of glycine at the C-cap terminal portions of alpha-helices have invoked uniquely favorable energetics of this residue in a left-handed conformation or enhanced solvation of the peptide backbone because of the absence of a side chain. Attempts to quantify the contributions of these two effects have been made previously, but the issue remains unresolved. Here we have used chemical protein synthesis to dissect the energetic basis of alpha-helix termination by comparing a series of ubiquitin variants containing an L-amino acid or the corresponding D-amino acid at the C-cap Gly35 position. D-Amino acids can adopt a left-handed conformation without energetic penalty, so the contributions of conformational strain and backbone solvation can thus be separated. Analysis of the thermodynamic data revealed that the preference for glycine at the C' position of a helix is predominantly a conformational effect.
About this StructureAbout this Structure
2FCQ is a Single protein structure. Full crystallographic information is available from OCA.
ReferenceReference
Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis., Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI, Nat Chem Biol. 2006 Mar;2(3):139-43. Epub 2006 Jan 30. PMID:16446709 Page seeded by OCA on Sun May 4 03:44:31 2008