John A. Tainer

ORCID: 0000-0003-1659-2429
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About
Contact & Profiles
Research Areas
  • DNA Repair Mechanisms
  • Enzyme Structure and Function
  • DNA and Nucleic Acid Chemistry
  • RNA and protein synthesis mechanisms
  • CRISPR and Genetic Engineering
  • Bacterial Genetics and Biotechnology
  • Metal-Catalyzed Oxygenation Mechanisms
  • Protein Structure and Dynamics
  • Nitric Oxide and Endothelin Effects
  • Genomics and Chromatin Dynamics
  • RNA modifications and cancer
  • Glycosylation and Glycoproteins Research
  • PARP inhibition in cancer therapy
  • Monoclonal and Polyclonal Antibodies Research
  • Bacteriophages and microbial interactions
  • Advanced biosensing and bioanalysis techniques
  • Photosynthetic Processes and Mechanisms
  • Biochemical and Molecular Research
  • Cancer-related Molecular Pathways
  • Mitochondrial Function and Pathology
  • RNA Research and Splicing
  • Glutathione Transferases and Polymorphisms
  • Ubiquitin and proteasome pathways
  • Microtubule and mitosis dynamics
  • Amyotrophic Lateral Sclerosis Research

The University of Texas MD Anderson Cancer Center
2016-2025

Lawrence Berkeley National Laboratory
2016-2025

The University of Texas Health Science Center at Houston
2022

Massachusetts Institute of Technology
1998-2022

Anderson University - South Carolina
2020

Washington University in St. Louis
2017

University of California, Santa Cruz
2017

Molecular Biology Consortium
2017

Scripps Research Institute
2006-2015

QB3
2013

Crystal structures of the murine cytokine-inducible nitric oxide synthase oxygenase dimer with active-center water molecules, substrate l -arginine ( -Arg), or product analog thiocitrulline reveal how dimerization, cofactor tetrahydrobiopterin, and -Arg binding complete catalytic center for synthesis essential biological signal cytotoxin oxide. Pterin refolds central interface region, recruits new structural elements, creates a 30 angstrom deep channel, causes 35° helical tilt to expose heme...

10.1126/science.279.5359.2121 article EN Science 1998-03-27

A major challenge in structural biology is to characterize structures of proteins and their assemblies solution. At low resolution, such a characterization may be achieved by small angle x-ray scattering (SAXS). Because SAXS analyses often require comparing profiles calculated from many atomic models against those determined experiment, rapid accurate profile computation molecular needed. We developed fast open-source (FoXS) for computation. To match the experimental within noise, FoXS...

10.1016/j.bpj.2013.07.020 article EN publisher-specific-oa Biophysical Journal 2013-08-01

Abstract Unstructured proteins, RNA or DNA components provide functionally important flexibility that is key to many macromolecular assemblies throughout cell biology. As objective, quantitative experimental measures of and disorder in solution are limited, small angle scattering (SAS), particular X‐ray (SAXS), provides a critical technology assess as well shape assembly. Here, we consider the Porod‐Debye law powerful tool for detecting biopolymer SAS experiments. We show region...

10.1002/bip.21638 article EN Biopolymers 2011-04-20

Small Angle X-ray Scattering (SAXS) is an increasingly common and useful technique for structural characterization of molecules in solution. A SAXS experiment determines the scattering intensity a molecule as function spatial frequency, termed profile. Here, we describe three web servers modeling atomic structures based on profiles. FoXS (Fast X-Ray Scattering) rapidly computes profile given atomistic model fits it to experimental FoXSDock docks two rigid protein their complex. MultiFoXS...

10.1093/nar/gkw389 article EN cc-by-nc Nucleic Acids Research 2016-05-05
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