Expertise Term: tertiary structure
 NameInstitutionRole
Campbell, SharonUniversity of North Carolina at Chapel HillEditorial Board Member
 
 
Name: Campbell, Sharon
Role: Editorial Board Member
Email: campbesl@med.unc.edu
Institution: University of North Carolina at Chapel Hill
Department: Biochemistry and Biophysics
Subject Categories:
Expertise Terms: Biophysics, cell adhesion, cell adhesion proteins, cell signaling, cysteine oxidation, enzyme purification, enzyme structure, Escherichia coli (E. coli), fluorescence, focal adhesions, G protein, G-actin, GTPase, GTPase activating protein (GAP), GTPase Kras (KRAS), guanine nucleotide exchange factor (GEF), inositol phospholipid, NMR spectroscopy, nuclear magnetic resonance (NMR), nucleoside/nucleotide analogue, paxillin, phosphatidylinositide 3-kinase (PI 3-kinase), post translational modification, post-translational modification (PTM), protein chemical modification, protein purification, Rac (Rac GTPase), Raf kinase, Ras and Ras related GTPases, Ras protein, Ras-related protein 1 (Rap1), Signal Transduction, structural biology, tertiary structure, vinculin
Frueh, DominiqueJohns Hopkins University School of MedicineEditorial Board Member
 
 
Name: Frueh, Dominique
Role: Editorial Board Member
Email: dfrueh1@jhmi.edu
Institution: Johns Hopkins University School of Medicine
Department: Biophysics and Biophysical Chemistry
Subject Categories: Molecular Biophysics, Protein Structure and Folding
Expertise Terms: acyl carrier protein (ACP), adenylation domain, Biophysics, condensation domain, conformational change, cyclization domain, enzyme, enzyme catalysis, enzyme mechanism, enzyme structure, fluorescence anisotropy, kinetics, Michaelis-Menten, natural product biosynthesis, NMR methods, non-ribosomal peptide synthestases, nonribosomal peptide synthestases, nuclear magnetic resonance (NMR), peptide biosynthesis, peptide conformation, protein chemical modification, protein conformation, protein domain, protein dynamic, protein structure, structural biology, structure-function, tertiary structure, thioesterase
Orlova, ElenaBirkbeck College, LondonEditorial Board Member
 
 
Name: Orlova, Elena
Role: Editorial Board Member
Email: e.orlova@mail.cryst.bbk.ac.uk
Institution: Birkbeck College, London
Department: Biological Sciences
Subject Categories: Computational Biology, Molecular Biophysics, Protein Structure and Folding
Expertise Terms: bacteriophage, Cryo elecron microscopy, E1 helicase, electron microscopy (EM), electron tomography, herpesvirus, Image processing, Molecular Biology, p53, protein conformation, protein structure, ribosome function, ribosome structure, single particle analysis, structural biology, Structure of bacteriopahges, Structure of calcium or potassium channels, Structure of ribosomes, tertiary structure, type III secretion system (T3SS), type IV pili, virus assembly, virus structure
Otzen, DanielAarhus UniversityEditorial Board Member
 
 
Name: Otzen, Daniel
Role: Editorial Board Member
Email: dao@inano.au.dk
Institution: Aarhus University
Department:
Subject Categories: Molecular Biophysics
Expertise Terms: amyloid, membrane protein, micelle, neurodegenerative disease, Parkinson disease, phospholipid vesicle, pre-steady-state kinetics, protein aggregation, protein conformation, protein denaturation, protein engineering, protein folding, protein misfolding, protein self-assembly, protein stability, protein-lipid interaction, tertiary structure, transmembrane domain
Pearce, F. GrantUniversity of CanterburyEditorial Board Member
 
 
Name: Pearce, F. Grant
Role: Editorial Board Member
Email: grant.pearce@canterbury.ac.nz
Institution: University of Canterbury
Department:
Subject Categories: Enzymology, Molecular Biophysics, Plant Biology
Expertise Terms: Biophysics, enzyme, enzyme inhibitor, enzyme kinetics, enzyme structure, oligomerization, photosynthesis, plant biochemistry, protein purification, protein stability, protein structure, ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), small-angle X-ray scattering (SAXS), tertiary structure, ultracentrifugation
Williams, R.National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human ServicesEditorial Board Member
 
 
Name: Williams, R.
Role: Editorial Board Member
Email: williamsrs@niehs.nih.gov
Institution: National Institute of Environmental Health Sciences, National Institutes of Health, Department of Health and Human Services
Department: Genome Integrity and Structural Biology Laboratory
Subject Categories: DNA and Chromosomes, Molecular Bases of Disease, Protein Structure and Folding
Expertise Terms: ADP-ribosylation, Aprataxin, BRCA1, BRCT, cancer biology, cancer therapy, chromatin, chromatin modification, chromatin structure, chromosomes, crystal structure, crystallography, DNA, DNA binding protein, DNA damage, DNA damage response, DNA endonuclease, DNA enzyme, DNA repair, DNA topoisomerase, DNA-protein interaction, enzyme catalysis, enzyme mechanism, enzyme structure, genomic instability, Mre11, Nbs1, nucleic acid enzymology, nucleic acid structure, oncogene, polyubiquitin chain, proliferating cell nuclear antigen (PCNA), protein chemistry, protein crystallization, protein domain, protein engineering, protein phosphorylation, protein processing, protein structure, protein-DNA interaction, protein-nucleic acid interaction, protein-protein interaction, Rad50, radiation biology, recombination, small ubiquitin-like modifier (SUMO), small-angle X-ray scattering (SAXS), SUMO-interacting motif (SIM), sumoylation, tertiary structure, Tyrosyl DNA phosphodiesterase, ubiquitin ligase, ubiquitin-conjugating enzyme (E2 enzyme), X-ray crystallography, zinc finger