Open AccessPrediction of the Amount of Secondary Structure in a Globular Protein from Its Aminoacid Composition
Author(s) -
W. R. Krigbaum,
Sara Parkey Knutton
Publication year - 1973
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.70.10.2809
Subject(s) - globular protein , protein tertiary structure , protein secondary structure , composition (language) , protein structure , sequence (biology) , protein structure prediction , helix (gastropod) , protein folding , chemistry , biology , biophysics , crystallography , biochemistry , ecology , philosophy , linguistics , snail
Multiple regression is used to obtain relationships for predicting the amount of secondary structure in a protein molecule from a knowledge of its aminoacid composition. We tested these relations using 18 proteins of known structure, but omitting the protein to be predicted. Independent predictions were made for the two subchains of hemoglobin and insulin. The average errors for these 20 chains or subchains are: helix ± 7.1%, β-sheet ± 6.9%, turn ± 4.2%, and coil ± 5.7%. A second set of relations yielding somewhat inferior predictions is given for the case in which Asp and Asn, and Glu and Gln, are not differentiated. Predictions are also listed for 15 proteins for which the aminoacid sequence or tertiary structure is unknown.