Week 1
The attraction or repulsion of two atoms, molecules, or surfaces that generate a weak interaction when in close proximity.
What are van der Waals forces?
This atom in amino acids is asymmetric, allowing amino acids to exist as mirror-image stereoisomers, although proteins contain only the L form.
What is alpha carbon
The area of proteins that interact with a ligand.
What is the ligand binding site?
This basic unit of chromatin consists of DNA wrapped around a core of histone proteins and helps compact DNA within the nucleus.
What is a nucelosome
The long-term interaction of an ancient archaeal anaerobe that engulfed an aerobic bacterial cell, improving energy generation and providing mutual metabolic support.
What is an endosymbiotic relationship?
This secondary structure is stabilized by hydrogen bonding within a single polypeptide chain and can form amphiphilic structures with hydrophobic and hydrophilic faces.
What is alpha helix
This is a measure of protein-ligand binding strength, which can be calculated from the concentrations of unbound and bound proteins and ligands at equilibrium.
What is the equilibrium constant, K?
These chromosome regions are tightly packed, transcriptionally inactive, and often enriched near centromeres and telomeres.
What is heterochromatin
When two or more existing genes break and rejoin to form a hybrid gene consisting of DNA segments that originally belonged to separate genes.
What is DNA segment shuffling?
These weak interactions, including hydrogen bonds and van der Waals forces, collectively stabilize protein structure and molecular interactions.
What are noncovalent bonds
A control mechanism where something that is not a substrate binds to an enzyme at the regulatory site and it discourages the enzyme/substrate interactions.
What is feedback inhibition or negative regulation?
This is the space between the inner and outer nuclear member.
What is the endoplasmic reticulum?
A chemical reaction will occur spontaneously when this value is negative.
What is Gibbs free energy (ΔG)?
This amino acid is commonly known as a “helix breaker” because its rigid ring structure disrupts the hydrogen bonding pattern of alpha helices.
What is proline
This enzyme catalyzes the addition of a phosphate group from ATP to the hydroxyl group of a serine, threonine, or tyrosine protein side chain.
What is a protein kinase?
The evolutionary molecular clock runs faster when in DNA sequences not subjected to this.
What is purifying selection?
The reaction that occurs with two atoms that require the transfer of electrons, specifically involves the loss of electrons.
What is oxidation?
This process occurs when proteins misfold and aggregate into amyloid structures, contributing to diseases such as Parkinson’s
What is the protein misfolding/aggregates
GTP hydrolysis causes this tertiary structure to conformationally change from a shut to an open position on EF-Tu.
What is the switch helix?
This coiled-coil dimer protein ring structure binds to the DNA double helix, providing organization for chromosomal DNA.
What is the SMC (structural maintenance of chromosomes) protein complex?