5HFY

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

Summary for 5HFY

Entry DOI	10.2210/pdb5hfy/pdb
Related	5HI1 5HI2
Descriptor	Immunoglobulin G-binding protein G (2 entities in total)
Functional Keywords	synthetic protein, de novo protein
Biological source	Streptococcus sp. group G
Cellular location	Secreted, cell wall ; Peptidoglycan-anchor : P19909
Total number of polymer chains	2
Total formula weight	12475.55
Authors	Tavenor, N.A.,Reinert, Z.E.,Lengyel, G.A.,Griffith, B.D.,Horne, W.S. (deposition date: 2016-01-07, release date: 2016-02-24, Last modification date: 2023-11-15)
Primary citation	Tavenor, N.A.,Reinert, Z.E.,Lengyel, G.A.,Griffith, B.D.,Horne, W.S. Comparison of design strategies for alpha-helix backbone modification in a protein tertiary fold. Chem.Commun.(Camb.), 52:3789-3792, 2016 Cited by PubMed Abstract: We report here the comparison of five classes of unnatural amino acid building blocks for their ability to be accommodated into an α-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 α-helix mimetics and suggest refined design rules for engineering the backbones of natural sequences. PubMed: 26853882 DOI: 10.1039/c6cc00273k PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation