Jeffrey W. Peng

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BACKGROUND Recently, it has been shown that nuclear magnetic resonance (NMR) may be used to identify ligands that bind to low molecular weight protein drug targets. Recognizing the utility of NMR as a very sensitive method for detecting binding, we have focused on developing alternative approaches that are applicable to larger molecular weight drug targets(More)
The self-assembly of the soluble peptide Abeta into Alzheimer's disease amyloid is believed to involve a conformational change. Hence the solution conformation of Abeta is of significant interest. In contrast to studies in other solvents, in water Abeta is collapsed into a compact series of loops, strands, and turns and has no alpha-helical or beta-sheet(More)
Osteoblasts are essential for maintaining bone mass, avoiding osteoporosis, and repairing injured bone. Activation of osteoblast G protein-coupled receptors (GPCRs), such as the parathyroid hormone receptor, can increase bone mass; however, the anabolic mechanisms are poorly understood. Here we use "Rs1," an engineered GPCR with constitutive G(s) signaling,(More)
The DNA binding domain (residues 1--65) of the yeast transcriptional activator GAL4 is only partially folded. While residues 10-41, the DNA recognition domain, form a well-defined structure in the free protein, the whole polypeptide folds up and dimerizes upon binding DNA. In order to describe the mobility of the protein, we have characterized the frequency(More)
A method is proposed for direct mapping of spectral density functions of the rotational motions of H-X bond vectors, such as ‘H-“N, by measuring a set of NMR relaxation parameters. The well known and frequently measured relaxation parameters T, and T, probe the spectral density function J(o) at five frequencies: 0, WN, wn, in wN, and wu t wN. In this study,(More)
3.1. Fast Exchange Approximation 3645 4. Ligand-Based versus Receptor-Based Screening 3646 5. Ligand-Based NMR Screening Methods 3646 5.1. Transverse Relaxation Rates 3647 5.2. Longitudinal Relaxation Rates 3649 5.3. Paramagnetic Relaxation Enhancements 3649 5.4. 19F Relaxation 3650 5.5. Saturation Transfer Difference (STD) Methods 3650 5.6. WaterLOGSY 3653(More)
The internal mobility of the protein eglin c is characterized with spectral density functions of the NH vectors obtained from heteronuclear NMR relaxation at multiple field strengths (7.04, 11.74, and 14.1 T). The spectral density functions, J(omega), describe the frequency spectrum of the rotational fluctuations of the XH bond vectors (15N-1H and 13C-1H).(More)
A new strategy is used for studying the internal motions of proteins based on measurements of NMR relaxation parameters. The strategy yields values of the so-called spectral density functions J(omega) for N-H bond vectors. The spectral density functions are related to the distribution of frequencies contained in the rotational (overall and internal) motions(More)
The amyloid Abeta(10-35)-NH2 peptide is simulated in an aqueous environment on the nanosecond time scale. One focus of the study is on the validation of the computational model through a direct comparison of simulated statistical averages with experimental observations of the peptide's structure and dynamics. These measures include (1) nuclear magnetic(More)