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Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
In a designed fusion protein the trimeric domain foldon from bacteriophage T4 fibritin was connected to the C terminus of the collagen model peptide (GlyProPro)(10) by a short Gly-Ser linker to facilitate formation of the three-stranded collagen triple helix. Crystal structure analysis at 2.6 A resolution revealed conformational changes within the interface of both domains compared with the structure of the isolated molecules. A striking feature is an angle of 62.5 degrees between the symmetry axis of the foldon trimer and the axis of the triple helix. The melting temperature of (GlyProPro)(10) in the designed fusion protein (GlyProPro)(10)foldon is higher than that of isolated (GlyProPro)(10,) which suggests an entropic stabilization compensating for the destabilization at the interface.
Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon.,Stetefeld J, Frank S, Jenny M, Schulthess T, Kammerer RA, Boudko S, Landwehr R, Okuyama K, Engel J Structure. 2003 Mar;11(3):339-46. PMID:12623021[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Stetefeld J, Frank S, Jenny M, Schulthess T, Kammerer RA, Boudko S, Landwehr R, Okuyama K, Engel J. Collagen stabilization at atomic level: crystal structure of designed (GlyProPro)10foldon. Structure. 2003 Mar;11(3):339-46. PMID:12623021
