5hg2

Backbone Modifications in the Protein GB1 Helix: beta-3-Ala24, beta-3-Lys28, beta-3-Lys31, beta-2-Asn35

spinqualitylabelsall models 5hg2, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Method: X-ray diffraction, Resolution 1.8Å Ligands: B2N, B3A, B3K, GOL, MG, NH2 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein G

Proteopedia Page Contributors and Editors (what is this?)

OCA