Amino acid residue volumes

Range Table - link 10^-3×nm^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.172 table 1PubMed ID3709531
Primary Source See refs beneath table
Method See top row in table
Comments P.171 right column 4th paragraph:"Amino acid residue volumes are compared in Table 1. The residues are arranged in order of decreasing hydrophobicity to follow the consensus hydrophobicity scale of Eisenberg [ref 68]. The classical 1943 Cohn-Edsall compilation (Table 1) was obtained from densitometric studies of eight free amino acids and molar group summations for the other twelve amino acids. The original value for Cys was 103.3x10^-3nm^3 [primary source 3] however, this was based on a calculation error and was corrected later on [refs 69,70] to give 106.7x10^-3nm^3 which is used here (Table 1). Since that time, full residue compilations can be derived by four independent approaches based on densitometry, molar group summations, protein crystal structures, and amino acid crystal structures. Five further compilations from these are given in Table 1."
Entered by Uri M
ID 112196