Assignment of protein backbone resonances using connectivity, torsion angles and 13C[alpha] chemical shifts

• Published in: Journal of biomolecular NMR Vol. 29; no. 1; p. 1
• Main Authors: Morris, Laura C, Valafar, Homayoun, Prestegard, James H
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Nature B.V 01.05.2004
• Subjects: Amino acids; Proteins; Studies
• ISSN: 0925-2738; 1573-5001
• DOI: 10.1023/B:JNMR.0000019500.76436.31

A program is presented which will return the most probable sequence location for a short connected set of residues in a protein given just ^sup 13^C^sup α^ chemical shifts (δ(^sup 13^C^sup α^)) and data restricting the Φ and ψ backbone angles. Data taken from both the BioMagResBank and the Protein Data Bank were used to create a probability density function (PDF) using a multivariate normal distribution in δ(^sup 13^C^sup α^), Φ, and ψ space for each amino acid residue. Extracting and combining probabilities for particular amino acid residues in a short proposed sequence yields a score indicative of the correctness of the proposed assignment. The program is illustrated using several proteins for which structure and ^sup 13^C^sup α^ chemical shift data are available.[PUBLICATION ABSTRACT]