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• W2069177550 startingPage "6019" @default.
• W2069177550 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." @default.
• W2069177550 created "2016-06-24" @default.
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• W2069177550 date "1984-10-01" @default.
• W2069177550 modified "2023-10-15" @default.
• W2069177550 title "Dynamic filtering by two-dimensional 1H NMR with application to phage lambda repressor." @default.
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• W2069177550 doi "https://doi.org/10.1073/pnas.81.19.6019" @default.
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