Mary R. Starich

ORCID: 0000-0002-8603-4628
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About
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Research Areas
  • RNA and protein synthesis mechanisms
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Bacteriophages and microbial interactions
  • Protein Interaction Studies and Fluorescence Analysis
  • Metal complexes synthesis and properties
  • RNA modifications and cancer
  • Genomics and Chromatin Dynamics
  • Plant Virus Research Studies
  • Lanthanide and Transition Metal Complexes
  • RNA Research and Splicing
  • Molecular Biology Techniques and Applications
  • Advanced NMR Techniques and Applications
  • Bacterial Genetics and Biotechnology
  • Glycosylation and Glycoproteins Research
  • S100 Proteins and Annexins
  • Research in Cotton Cultivation
  • Plant biochemistry and biosynthesis
  • Biopolymer Synthesis and Applications
  • Insect Utilization and Effects
  • Complement system in diseases
  • Signaling Pathways in Disease
  • DNA and Nucleic Acid Chemistry
  • Enzyme-mediated dye degradation
  • Photosynthetic Processes and Mechanisms

National Heart Lung and Blood Institute
2018-2024

National Institutes of Health
1999-2024

National Cancer Institute
2006-2009

Frederick National Laboratory for Cancer Research
2009

University of California, Santa Barbara
2006

National Institute of Diabetes and Digestive and Kidney Diseases
1998-1999

University of Maryland, Baltimore County
1994-1996

Howard Hughes Medical Institute
1994-1996

University of Utah
1994

University of Wisconsin–Milwaukee
1991

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTMeasurement of Residual Dipolar Couplings Macromolecules Aligned in the Nematic Phase a Colloidal Suspension Rod-Shaped VirusesG. Marius Clore, Mary R. Starich, and Angela M. GronenbornView Author Information Laboratory Chemical Physics, Building 5, National Institute Diabetes Digestive Kidney Diseases Institutes Health, Bethesda, Maryland 20892-0520 Cite this: J. Am. Chem. Soc. 1998, 120, 40, 10571–10572Publication Date (Web):September 24,...

10.1021/ja982592f article EN Journal of the American Chemical Society 1998-09-24

The 3 ′ untranslated region (3 UTR) of turnip crinkle virus (TCV) genomic RNA contains a cap-independent translation element (CITE), which includes ribosome-binding structural (RBSE) that participates in recruitment the large ribosomal subunit. In addition, symmetric loop RBSE plays key role coordinating incompatible processes viral and replication, require enzyme progression opposite directions on template. To understand basis for subunit intricate interplay among different parts molecule,...

10.1073/pnas.0908140107 article EN Proceedings of the National Academy of Sciences 2010-01-07

Folded proteins are assumed to be built upon fixed scaffolds of secondary structure, α-helices and β-sheets. Experimentally determined structures >58,000 non-redundant support this assumption, though it has recently been challenged by ~100 fold-switching proteins. Though ostensibly rare, these raise the question how many uncharacterized have shapeshifting-rather than fixed-secondary structures. Here, we use a comparative sequence-based approach predict fold switching in universally conserved...

10.1038/s41467-022-31532-9 article EN cc-by Nature Communications 2022-07-01

S100B(ββ), a member of the S100 protein family, is Ca2+-binding with noncovalent interactions at its dimer interface. Each apo-S100β subunit (91 residues) has four α-helices and small antiparallel β-sheet, consistent two predicted helix−loop−helix domains known as EF-hands [Amburgey et al. (1995) J. Biomol. NMR 6, 171−179]. The three-dimensional solution structure apo-S100B(ββ) from rat been determined using 2672 distance (14.7 per residue) 88 dihedral angle restraints derived...

10.1021/bi9612226 article EN Biochemistry 1996-01-01

ADVERTISEMENT RETURN TO ISSUEPREVCommunicationNEXTImpact of Residual Dipolar Couplings on the Accuracy NMR Structures Determined from a Minimal Number NOE RestraintsG. Marius Clore, Mary R. Starich, Carole A. Bewley, Mengli Cai, and John KuszewskiView Author Information Laboratory Chemical Physics, Building 5 National Institute Diabetes Digestive Kidney Diseases Institutes Health Bethesda, Maryland 20892-0520 Cite this: J. Am. Chem. Soc. 1999, 121, 27, 6513–6514Publication Date (Web):June...

10.1021/ja991143s article EN Journal of the American Chemical Society 1999-06-25

Beetroot is a homodimeric in vitro selected RNA that binds and activates DFAME, conditional fluorophore derived from GFP. It 70% sequence-identical to the previously characterized aptamer Corn, which one molecule of its cognate DFHO at interprotomer interface. We have now determined Beetroot-DFAME co-crystal structure 1.95 Å resolution, discovering this homodimer two molecules fluorophore, sites separated by ~30 Å. In addition overall architectural difference, local structures non-canonical,...

10.1038/s41467-023-38683-3 article EN cc-by Nature Communications 2023-05-23

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTOxidation of the phosphine from auranofin analog, triisopropylphosphine(2,3,4,6-tetra-O-acetyl-1-thio-.beta.-D-glucopyranosato-S)gold(I), via a protein-bound phosphonium intermediateC. Frank Shaw III, Anvarhusein A. Isab, James D. Hoeschele, Mary Starich, Locke, Pamela Schulteis, and Jun XiaoCite this: J. Am. Chem. Soc. 1994, 116, 6, 2254–2260Publication Date (Print):March 1, 1994Publication History Published online1 May 2002Published inissue 1...

10.1021/ja00085a003 article EN Journal of the American Chemical Society 1994-03-01

Abstract The odorant binding protein, OBP44a is one of the most abundant proteins expressed in brain developing fruit fly Drosophila melanogaster . Its cellular function has not yet been determined. OBP family well established to recognize hydrophobic molecules. In this study, NMR employed structurally characterize OBP44a. chemical shift perturbation measurements confirm that binds fatty acids. Complete assignments backbone shifts and secondary analysis demonstrate apo state comprised six...

10.1007/s12104-024-10178-2 article EN cc-by Biomolecular NMR Assignments 2024-06-01

Regulating the activity of histidine autokinase CheA is a central step in bacterial chemotaxis. The autophosphorylation reaction minimally involves two domains, denoted P1 and P4. kinase domain (P4) binds adenosine triphosphate (ATP) orients γ phosphate for phosphotransfer to reactive on phosphoacceptor (P1). Three-dimensional triple-resonance experiments allowed sequential assignments backbone nuclei from P4 domains as well within larger construct, P3P4, which includes dimerization P3. We...

10.1021/bi060798k article EN Biochemistry 2006-07-13

Summary Hundreds of millions structured proteins sustain life through chemical interactions and catalytic reactions 1 . Though dynamic, these are assumed to be built upon fixed scaffolds secondary structure, α-helices β-sheets. Experimentally determined structures over >58,000 non-redundant support this assumption, though it has recently been challenged by ∼100 fold-switching 2 These “metamorphic 3 ” proteins, ostensibly rare, raise the question how many uncharacterized have...

10.1101/2021.06.10.447921 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-06-11
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