Biomaterial Database

Prediction of the helix/strand content of globular proteins based on their primary sequences. 1998

C T Zhang, and Z S Lin, and Z Zhang, and M Yan

Department of Physics, Tianjin University, China.

An improved multiple linear regression method has been proposed to predict the content of alpha-helix and beta-strand of a globular protein based on its primary sequence. The amino acid composition and the auto-correlation functions based on the hydrophobicity profile of the primary sequence have been taken into account in the algorithm. The resubstitution test shows that the average absolute errors are 0.077 and 0.073 with the standard deviations 0.059 and 0.057 for the prediction of the content of alpha-helix and beta-strand, respectively. A stringent cross-validation test, i.e., the jackknife test, shows that the average absolute errors are 0.087 and 0.081 with the standard deviations 0.067 and 0.065 for the prediction of the content of alpha-helix and beta-strand, respectively. Both tests indicate the self-consistency and the extrapolating effectiveness of the new algorithm. This greatly improves on previous results (Eisenhaber,F., Imperiale,F., Argos,P. and Frommel,C., 1996, Proteins, 25, 157-168). Compared with other methods currently available, our method has the merits of simplicity and ease-of-use as well as a higher prediction accuracy. The only input of the method is the primary sequence of the query protein to be predicted. The program is available on request via e-mail: ctzhang@tju.edu.cn.

UI	MeSH Term	Description	Entries
D011506	Proteins	Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.	Gene Products, Protein,Gene Proteins,Protein,Protein Gene Products,Proteins, Gene
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D017433	Protein Structure, Secondary	The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation.	Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein