Structural highlights
5hg2 is a 4 chain structure with sequence from Streptococcus sp. 'group G'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Method: | X-ray diffraction, Resolution 1.8Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
SPG2_STRSG
Publication Abstract from PubMed
We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an alpha-helix in a protein tertiary fold context. High-resolution structural characterization and analysis of folding thermodynamics yield new insights into the relationship between backbone composition and folding energetics in alpha-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences.
Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold.,Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS Chem Commun (Camb). 2016 Feb 25;52(19):3789-92. doi: 10.1039/c6cc00273k. PMID:26853882[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tavenor NA, Reinert ZE, Lengyel GA, Griffith BD, Horne WS. Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold. Chem Commun (Camb). 2016 Feb 25;52(19):3789-92. doi: 10.1039/c6cc00273k. PMID:26853882 doi:http://dx.doi.org/10.1039/c6cc00273k
