A5061288516- Protein Structure and Dynamics
- Enzyme Structure and Function
- Hemoglobin structure and function
- Advanced NMR Techniques and Applications
- RNA and protein synthesis mechanisms
- DNA and Nucleic Acid Chemistry
- RNA Research and Splicing
- Molecular spectroscopy and chirality
- Photosynthetic Processes and Mechanisms
- NMR spectroscopy and applications
- Genomics and Chromatin Dynamics
- Cancer-related Molecular Pathways
- Monoclonal and Polyclonal Antibodies Research
- Neonatal Health and Biochemistry
- Chemical Synthesis and Analysis
- Amyloidosis: Diagnosis, Treatment, Outcomes
- Glycosylation and Glycoproteins Research
- Electron Spin Resonance Studies
- Cancer-related gene regulation
- Mass Spectrometry Techniques and Applications
- Porphyrin Metabolism and Disorders
- Metabolomics and Mass Spectrometry Studies
- RNA modifications and cancer
- Ubiquitin and proteasome pathways
- Hippo pathway signaling and YAP/TAZ
Scripps Research Institute
2016-2025
Scripps Institution of Oceanography
2020-2023
University of Illinois at Springfield
2022
Durrell Wildlife Conservation Trust
2019
Science Oxford
2019
University of Toronto
2001-2016
Institut de Biologie Structurale
2013
European Molecular Biology Laboratory
2013
Université Grenoble Alpes
2013
Centre National de la Recherche Scientifique
2013
We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in the catalytic cycle samples low-lying excited states whose conformations resemble ground-state structures preceding and following intermediates. Substrate cofactor exchange occurs through these substates. The maximum hydride transfer steady-state turnover rates are governed by dynamics transitions between ground...
Hydrogen exchange pulse labeling and stopped-flow circular dichroism were used to establish that the structure of earliest detectable intermediate formed during refolding apomyoglobin corresponds closely a previously characterized equilibrium molten globule. This compact, cooperatively folded was in less than 5 milliseconds contained stable, hydrogen-bonded secondary localized A, G, H helices part B helix. The remainder helix on much slower time scale, followed by C E CD loop. data indicate...
To understand why proteins adopt particular three-dimensional structures, it is important to elucidate the hierarchy of interactions that stabilize native state. Proteins in partly folded states can be used dissect protein organizational hierarchies. A apomyoglobin intermediate has now been characterized structurally by trapping slowly exchanging peptide NH protons and analyzing them two-dimensional 1 H-NMR (nuclear magnetic resonance). Protons A, G, H helix regions are protected from...
The prion diseases seem to be caused by a conformational change of the protein (PrP) from benign cellular form PrP C infectious scrapie Sc ; thus, detailed information about structure may provide essential insights into mechanism which these develop. In this study, secondary recombinant Syrian hamster residues 29–231 [PrP(29–231)] is investigated multidimensional heteronuclear NMR. Chemical shift index analysis and nuclear Overhauser effect data show that PrP(29–231) contains three helices...
The three-dimensional solution structure of a zinc finger nucleic acid binding motif has been determined by nuclear magnetic resonance (NMR) spectroscopy. Spectra synthetic peptide corresponding to single from the Xenopus protein Xfin yielded distance and dihedral angle constraints that were used generate structures geometry restrained molecular dynamics calculations. is an independently folded domain with compact globular in which atom bound two cysteine histidine ligands. polypeptide...
Random coil chemical shifts are commonly used to detect secondary structure elements in proteins shift index calculations. While this technique is very reliable for folded proteins, application unfolded reveals significant deviations from measured random certain nuclei. some of these can be ascribed residual the protein, others clearly caused by local sequence effects. In particular, amide nitrogen, proton, and carbonyl carbon highly sensitive amino acid sequence. We present a detailed,...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTIntramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopyArthur G. Palmer III, Mark Rance, and Peter E. WrightCite this: J. Am. Chem. Soc. 1991, 113, 12, 4371–4380Publication Date (Print):June 1, 1991Publication History Published online1 May 2002Published inissue 1 June...
The cyclin-dependent kinase (Cdk) inhibitor p21Waf1/Cip1/Sdi1, important for p53-dependent cell cycle control, mediates G1/S arrest through inhibition of Cdks and possibly DNA replication. Cdk requires a sequence approximately 60 amino acids within the p21 NH2 terminus. We show, using proteolytic mapping, circular dichroism spectropolarimetry, nuclear magnetic resonance spectroscopy, that NH2-terminal fragments are active as inhibitors lack stable secondary or tertiary structure in free...
Evidence is growing to support a functional role for the prion protein (PrP) in copper metabolism. Copper ions appear bind highly conserved octapeptide repeat region (sequence PHGGGWGQ) near N terminus. To delineate site and mode of binding Cu(II) PrP, copper-binding properties peptides varying lengths corresponding 2-, 3-, 4-octarepeat sequences have been probed by using various spectroscopic techniques. A two-octarepeat peptide binds single ion with K d ≈ 6 μM whereas four-octarepeat...