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Bioluminescence
The production and emission of light by a living organism.
Chemiluminescence
The emission of light as a result of a chemical reaction.
Aequorea victoria
A species of jellyfish that exhibits bioluminescence.
GFP (Green Fluorescent Protein)
A protein isolated from Aequorea victoria that absorbs blue light (475nm) and emits green light (510nm)
238 AA peptide
Fluoresce originates from Ser - Tyr - Gly Tripeptide
Photophysics
The study of the physical properties and behavior of light.
X-ray crystallography
A technique used to determine the atomic and molecular structure of a crystal.
Tripeptide
A peptide consisting of three amino acids.
Post-translational modification
Chemical modifications that occur to a protein after it has been synthesized.
EGFP (Enhanced Green Fluorescent Protein)
A variant of GFP with improved spectral properties.
FP Spectral Variants
Variants of fluorescent proteins that exhibit different colors and characteristics.
Red Fluorescent Proteins
Proteins isolated from corals that absorb green light and fluoresce red.
FRET (Fluorescence Resonance Energy Transfer)
A process in which energy is transferred between two fluorophores.
Biosensor
A device or construct that detects and measures biological molecules or processes.
Transgenic
Referring to an organism that has had foreign DNA inserted into its genome.
BRAINBOW
A technique used to label neurons with multiple distinct colors to visualize synaptic circuits.
Genetically Encoded FRET Biosensors
Biosensors that utilize genetically encoded fluorescent proteins for FRET measurements.1. Osamu Shimomura:A scientist who discovered aequorin and GFP in 1961.
GFP
Green Fluorescent Protein, a protein that emits green light when exposed to certain wavelengths.
Martin Chalfie
A scientist from Columbia University who studied C. elegans nerve cells using GFP in the 1980s.
Douglas Prasher
A scientist from Woods Hole Oceanographic Institute who sequenced the GFP gene.
E.coli
The first organism in which GFP was used.
Roger Tsien
A scientist from the University of California, San Diego who made modifications to GFP.
Tulle Hazelrigg
A scientist from Columbia University who studied fusion proteins in Drosophila (fruit fly) and preserved the structure and function of both proteins.
Protein Structure
The arrangement of amino acids in a protein molecule.
Enzymes
Proteins that catalyze chemical reactions in living organisms.
Defence
Proteins, such as antibodies, that protect the body against foreign substances.
Structure
Proteins, like collagen, that provide support and shape to cells and tissues.
Storage
Proteins, like ovalbumin, that store nutrients for later use.
Transport
Proteins, like hemoglobin, that carry molecules and ions throughout the body.
Movement
Proteins, like actin and myosin, that enable muscle contraction and movement.
Regulation/Receptors
Proteins, like insulin and insulin receptors, that control and respond to signals in the body.
Amino Acid
The building blocks of proteins.
Hydrophobic
Amino acids with non-polar side chains that repel water.
Polar
Amino acids with polar side chains that attract water.
Acidic
Amino acids with negatively charged side chains.
Basic
Amino acids with positively charged side chains.
Hydropathy Scale
A scale that measures the hydrophobicity or hydrophilicity of amino acids.
Peptide Bond
The bond formed between two amino acids during protein synthesis.
Ramachandran Plot
A plot that shows the allowed regions of dihedral angles for amino acids in proteins.
Structural Motifs
Short segments of protein 3D structure that are spatially close but not necessarily adjacent in the sequence.
Tertiary Structure
The overall 3D structure of a single protein molecule.
Quaternary Structure
The arrangement of multiple protein subunits in a complex.
Post-Translational Modifications
Chemical modifications that occur after protein synthesis.
Phosphorylation
The addition of a phosphate group to a protein, often used for regulation.
Glycosylation
The addition of saccharide groups to a protein, affecting folding, stability, and regulation.
Acetylation
The addition of an acetyl group to a protein, often used for regulation.
Hydroxylation
The addition of a hydroxyl group to a protein, affecting regulation.
Methylation
The addition of a methyl group to a protein, often used for regulation.
Disulfide Bonds
Covalent bonds formed between two cysteine residues, contributing to protein stability.
Ubiquitination
The attachment of ubiquitin molecules to a protein, marking it for degradation.
Polymorphic
Proteins with sequence variability among individuals.
Site-directed Mutagenesis
A technique used to introduce specific mutations into a protein's DNA sequence for studying structure and function.1. Extracellular fluid (ECF):The fluid surrounding cells from which they acquire molecules and ions.
Diffusion
The spontaneous movement of molecules and ions down their concentration gradient.
Active transport
The movement of molecules and ions against their concentration gradient, requiring the expenditure of energy.
Electrochemical gradient/potential
The combination of the chemical gradient (difference in solute concentrations) and the electrical gradient (difference in potential/charge) across a membrane.
Resting potential
The static membrane potential of quiescent cells.
Action potential
The rapid rise and fall of membrane potential in a specific cell location, causing adjacent locations to similarly depolarize.
Voltage-gated ion channels
Channels in the plasma membrane of cells that open and close in response to changes in membrane potential.
Selectivity filter
A segment in voltage-gated ion channels that allows the selective passage of specific ions.
Ion pore domain
A structural component of voltage-gated ion channels that forms the ion-conducting pore.
Voltage sensor
A component of voltage-gated ion channels that detects changes in membrane potential and triggers channel opening or closing.
Tetramerization
The process of four identical subunits coming together to form a functional channel.
Patch clamping
A technique used to record the activity of individual ion channels.
Ion-selective micro-electrodes
Electrodes used to measure the concentration of specific ions.
X-ray crystallography
A method used to determine the three-dimensional structure of molecules, including ion channels.
Bacterial KcsA Channel
An experimental model used to study the structure and function of potassium channels.
Subunit structure
The organization of different segments within a potassium channel, including the selectivity filter, cavity, and internal pore.
Ion selectivity
The ability of a channel to selectively allow the passage of certain ions while excluding others.
Conformational change
A change in the three-dimensional structure of a molecule or protein.
Newton's cradle
A physical demonstration of the conservation of momentum, used here to describe the oscillation of potassium ions within the selectivity filter.
Vestibules
Large openings or chambers in ion channels.
Coordination geometry
The arrangement of atoms and their bonding in a molecule or ion.1. Rod MacKinnon:A scientist known for his work on ion channels.
Ion Channels
Protein structures that allow the flow of ions across cell membranes.
Reason to purify proteins
To provide material for structural or functional studies
Truly accurate method for determination of protein conc.
AA analysis on the hydrolysate
Mostly used for determination of protein conc.
Bovin serum albumin (BSA)
Low cost, high purity, ready availability
Ultraviolet absorption
Method for determination of protein conc, non-destructive, can be measured continuously, readily available
Lowry method, bicimchoninic method, Bradford method
Used to determine protein conc
Buffer composition (P. Isolation)
Ionic strength (0.1-0.2M)
PH (7-8)
Mostly Tris or phosphate
Anti oxidant
Buffer add
to prevent inter-/intramolecular disulphide bridges & oxidation
Enzyme inhibitors (buffer)
Protease inhibitors
Enzyme substrate & cofactors
Buffer add
EDTA
buffer add
To remove divalent metal ions
PVP
buffer add: plant tissue
To absorb phenolic compounds
Sodium azide
buffer add
Bacteriostatic agent