Average crystallographic measurement of disulfide bonds in proteins

Value 5.5 Å
Organism Generic
Reference Ainavarapu SR et al., Contour length and refolding rate of a small protein controlled by engineered disulfide bonds. Biophys J. 2007 Jan 1 92(1):225-33 p.229 right column top paragraphPubMed ID17028145
Primary Source [36] B.A. Katz, A. Kossiakoff The crystallographically determined structures of atypical strained disulfides engineered into subtilisin J. Biol. Chem., 261 (1986), pp. 15480-15485PubMed ID3096989
Comments P.229 right column top paragraph: "The assumption is that the intercept for the ΔLr data in Fig. 4 A corresponds to the distance between the α-carbon atoms of the cysteines, LSS, through the disulfide bond (Cα-Cβ-S-S-Cβ-Cα). However, the measured value of 4.3 aa × lr = 18 Å is in excess of the range expected from the average crystallographic measurement of disulfide bonds (5.5 Å) in proteins (primary source), suggesting that further elements are present in the protein structure."
Entered by Uri M
ID 114335