Assignment of protein backbone resonances using connectivity, torsion angles and 13C[alpha] chemical shifts
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 D...
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Published in | Journal of biomolecular NMR Vol. 29; no. 1; p. 1 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Dordrecht
Springer Nature B.V
01.05.2004
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Subjects | |
Online Access | Get full text |
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Summary: | 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] |
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ISSN: | 0925-2738 1573-5001 |
DOI: | 10.1023/B:JNMR.0000019500.76436.31 |