Dr. Linda K Tamm PSY D
Psychologist
15 Clyde Rd Suite 102 Somerset NJ, 08873About
Dr. Linda Tamm is a psychologist practicing in Somerset, NJ. Dr. Tamm specializes in the treatment of mental health problems, and helps people to cope with their mental illnesses. As a psychologist, Dr. Tamm evaluates and treats patients through a variety of methods, most typically being psychotherapy or talk therapy. Patients usually visit Dr. Tamm because they have been experiencing depression, anxiety, stress or anger for a significant period of time and are seeking help. Psychologists may perform a variety of exams and assessments to diagnose a mental condition.
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Expert Publications
Data provided by the National Library of Medicine- Time-resolved distance determination by tryptophan fluorescence quenching: probing intermediates in membrane protein folding.
- Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism.
- Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent.
- Interaction of mutant influenza virus hemagglutinin fusion peptides with lipid bilayers: probing the role of hydrophobic residue size in the central region of the fusion peptide.
- Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers.
- Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin.
- Tethered polymer-supported planar lipid bilayers for reconstitution of integral membrane proteins: silane-polyethyleneglycol-lipid as a cushion and covalent linker.
- A host-guest system to study structure-function relationships of membrane fusion peptides.
- pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers.
- Structure of outer membrane protein A transmembrane domain by NMR spectroscopy.
- Reconstituted syntaxin1a/SNAP25 interacts with negatively charged lipids as measured by lateral diffusion in planar supported bilayers.
- Viral fusion peptides: a tool set to disrupt and connect biological membranes.
- Structure and assembly of beta-barrel membrane proteins.
- Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin.
- Peptide mimics of SNARE transmembrane segments drive membrane fusion depending on their conformational plasticity.
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