Volume of water molecule bound to an amino acid

Value 25.8 Å^3 Range: ±3.8 Å^3
Organism Generic
Reference Perkins SJ. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur J Biochem. 1986 May 15 157(1):169-80. p.170 left column 2nd paragraph from bottomPubMed ID3709531
Method X ray crystallography
Comments Comparisons of crystal volumes that differ only be the addition of H20 gave the H2O volume of 25.8±3.8×10^-3nm^3 (five values). This agrees well with volumes of 23.6±3.4×10^-3nm^3 (seven values) from carbohydrate crystal structures [Perkins 1981 PMID 6795354], 24.5±2.3×10^-3nm^3 (46 values) from the comparison of 187 anhydrous and hydrated inorganic salts [Leclaire, A. & Monier, J. C. (1982) Acta Crystallogr. 838,724- 727.] and 26.3±4.5×10^-3nm^3 as the mean of data on nine crystal forms of ice [Leclaire et al., 1982]. See BNID 105874, 106549
Entered by Uri M
ID 103763