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| [[Image:2fcn.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2fcn| PDB=2fcn | SCENE= }} | | {{STRUCTURE_2fcn| PDB=2fcn | SCENE= }} |
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| '''X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group'''
| | ===X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_16446709}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16446709 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16446709}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tereshko, V.]] | | [[Category: Tereshko, V.]] |
| [[Category: Ubiquitin]] | | [[Category: Ubiquitin]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:44:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:10:02 2008'' |