[Analysis of the spatial structure of proteins in terms of residue-residue contacts. II. Contact affinity].
The possibility of detecting the mutual amino acid residue affinity when protein three-dimensional structures are described in terms of residue-residue contact matrices is discussed. The hypothesis of the lack of affinity between amino acid residues is examined; the values of the pertinent elements of the overall residue-residue contact matrices prove not to be statistically different from random estimates in 91%; the chance hypothesis is rejected in 9% of cases, represented as a rule by residues with charged side groups, especially oppositely charged ones.
Rodionov
M A
MA
Gurevich
A V
AV
Galaktionov
S G
SG
D000596:Amino Acids / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D008956:Models, Chemical; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D000596:Amino Acids; D011506:Proteins
Analiz prostranstvennoĭ struktury belkov v terminakh matrits ostatok-ostatochnykh kontaktov. III. Srodstvo ostatkov.