An NMR approach is demonstrated for elucidating the conformation of a peptide when tightly bound to a protein. A 26-residue peptide derived from rabbit skeletal muscle myosin light chain kinase, comprising the binding site for calmdulin, was complexed with uniformly (>95%) 15Nand %enriched calmodulin. Improved isotope-filtered two-dimensional NMR techiques were developed for suppressing NMR cal...

The idea that reversible binding of a small inorganic ion can mimic covalent modification by phosphate is, at first, surprising. However, there is a fairly long history of using such compounds (aluminum fluoride and vanadate as well as beryllofluoride) to form complexes with nucleoside diphosphates at the active sites of ATPases and GTPases (1, 2, 6, 13). Indeed, it was in an attempt to form su...

We devised a single-step selection method to identify short sequences within the folded Rev response element (RRE) of the human immunodeficiency virus (HIV) RNA genome that are proximal and able to bind short oligonucleotides. The method employed a library of partially randomized tethered oligonucleotide probes (TOPs) complementary to all regions of the RRE and an RNase H cleavage assay which i...