Carnegie Mellon University

File(s) stored somewhere else

Please note: Linked content is NOT stored on Carnegie Mellon University and we can't guarantee its availability, quality, security or accept any liability.

MONTE: An automated Monte Carlo based approach to nuclear magnetic resonance assignment of proteins.

journal contribution
posted on 2003-01-01, 00:00 authored by T. Kevin Hitchens, Jonathan A. Lukin, Yiping Zhan, Scott A. McCallum, Gordon RuleGordon Rule

A general-purpose Monte Carlo assignment program has been developed to aid in the assignment of NMR resonances from proteins. By virtue of its flexible data requirements the program is capable of obtaining assignments of both heavily deuterated and fully protonated proteins. A wide variety of source data, such as inter-residue scalar connectivity, inter-residue dipolar (NOE) connectivity, and residue specific information, can be utilized in the assignment process. The program can also use known assignments from one form of a protein to facilitate the assignment of another form of the protein. This attribute is useful for assigning protein-ligand complexes when the assignments of the unliganded protein are known. The program can be also be used as an interactive research tool to assist in the choice of additional experimental data to facilitate completion of assignments. The assignment of a deuterated 45 kDa homodimeric Glutathione-S-transferase illustrates the principal features of the program.




Usage metrics


    Ref. manager