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. 1984 Oct;81(19):6019–6023. doi: 10.1073/pnas.81.19.6019

Dynamic filtering by two-dimensional 1H NMR with application to phage lambda repressor.

M A Weiss, J L Eliason, D J States
PMCID: PMC391850  PMID: 6237367

Abstract

Flexible regions of proteins play an important role in catalysis, ligand binding, and macromolecular interactions. Because of its enhanced sensitivity to motional narrowing, two-dimensional coupling constant J-correlated 1H NMR may be used to observe these regions selectively. Dynamic filtering is an intrinsic feature of this experiment because cross-peak amplitude decays rapidly as linewidths approach the coupling constant. We demonstrate here the flexibility of the NH2-terminal arm of phage lambda repressor, which is thought to wrap around the double helix in the repressor-operator complex. The assignment of arm resonances is made possible by the construction of mutant repressor genes containing successive NH2-terminal deletions.

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Selected References

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