section bank number 1 - Bio

kinase -

adds phosphate

phosphatase -

removes phosphate

synthase -

adds bonds (no ATP)

phosphorylase -

breaks bonds with PI

What is G-actin?

Monomeric (single-unit) actin

What is F-actin?

Filamentous actin (polymer of G-actin)

If G-actin decreases, what happens to F-actin?

F-actin increases (polymerization)

What happens to actin during contraction?

More F-actin (filament formation)

Does contraction correlate with more or less G-actin?

less G actin

F-actin / G-actin increases means what biologically?

More filament formation → more contraction (they are oppisite, more G actin means less F actin, more F actin means less G actin (increases in ratio)

Depolymerization means:

breaking filaments → into monomers (F actin decreses, G actin increases)

depolymerization -

G actin increases, F actin decreases

Intermediate -

integrity (structure/support); keratin

Thick filaments=

myosin (tension (muscle contraction)

microfilaments -

actin

microtubules -

tubulin

an amino acid can be phosphorylated if it

has an OH group

the process of joining many small molecules (monomers) together to form a large molecule (polymer)

polymerization

When you see:

• germ-free

• no colonization

• sterile

this means

no microbiota present

insulin

lower glucose

read this chart

- insulin - without insulin

+ insulin - with insulin

- acetate - without acetate

+ acetate - with acetate

What do antibiotics do to gut microbiota?

increase them

increased volume of adipocytes would do what

increase weight

Which amino acid contains an unbranched alkyl side chain?

alanine

The stereochemical designators α and β distinguish between:

epimers at an anomeric carbon atom

“What bond is cleaved” means

what bond is broken

what bonds do DNA form and what are they made out of

phosphodiester and oxygen bonds

how would you find the molecular weight of a tetramer of 288-residue amino acid

round - 300 = 30 dKa, tetramer - 4. 30×4 120

what does mean D64 and what would least alter its function

aspartic acid and glutamate since it is an acid

define denaturing, reducing, native

• Denaturing → breaks proteins apart

• Reducing → breaks disulfide bonds

• Native → keeps structure/complexes intact

in order to confirm that a small molecule induces the formation of integrase tetramers from integrase dimers, it is necessary to visualize the proteins

in their native state

• Unfold proteins → linear chains

• Used to measure:

  • Molecular weight (size)

denaturing (SDS)

• Break disulfide bonds

• Used when:

  • Subunits are linked by S–S bonds

reducing conditions (β-mercaptoethanol, DTT)

• Keep proteins folded and intact

• Used to study:

  • Oligomerization (dimers, tetramers)

  • Binding interactions

native conditions

gallblader -

stores bile

stomach -

produce hydrochloric acid (HCl) (parietal cells)

pancreas

secrete glucagon (alpha cells)

liver -

detoxify drugs

isoforms are produced through

alternative splicing of pre-mRNA

if something has cooperativty then hills coefficient should be

greater than 1

A characteristic of noncompetitive inhibitors is that they bind the

enzyme and the enzyme–substrate complex with the same affinity

CFU/mL = (colony forming units) =

amount of bacteria

Isoelectric focusing

separates amino acids by their isoelectric points (proteins move until they reach the spot where pH = their pl and net charge = 0 /they stop moving)

post-translational modification

That means:

• Protein is already made

• Then it gets modified (phosphorylation, etc.) which creats mkdified forms of the same protein

if PKA or GSK-3 autophosphorylate, what do they need in order to do that

ATP

Ovarian cells are

epithelial cells

osteoclasts are

connective tissue cells

When is uncompetitive inhibition most effective?

• High substrate concentration

• High inhibitor concentration

Why does uncompetitive inhibition increase with ↑ substrate?

• inhibitor binds ONLY to ES complex

• More substrate → more ES → more inhibition

Can adding substrate overcome uncompetitive inhibition?

no (opposite of competitive)

Why would a peptide homrone not need a transport protein?

peptides contain hydrophilic tails → soluble in blood

Which hormones need transport proteins?

Steroid hormones (lipophilic)

Do peptide hormones diffuse through membranes?

No → they use receptors (can’t cross membrane)

What tissue type are ovarian cells?

epithelial

What makes a GOOD control?

Removes the variable you're testing

How can one gene produce multiple proteins?

Alternative splicing (different exon combinations)

What level of protein structure affects binding interactions most?

Tertiary (3D folding)

Why might a full protein bind worse than a peptide fragment?

Tertiary structure blocks binding sites

What tissue type are osteoclasts?

connective (bone cells)

What does LOWER Kd mean?

higher affinity

How do you recognize higher affinity on a graph?v

binding happens at lower concentration

What mutation is detectable?

One that creates or destroys restriction site

What is a palindromic sequence?

Same forward/backward (e.g., GAATTC)

restriction enzymes recognize what?

Palindromic sequences

What is special about retroviruses?

RNA → DNA → integrates into host genome

If given mRNA, what matches viral genome?

Same sequence (still would contain U)

How do you detect different protein isoforms?

Look at mRNA differences (splicing)

Why is genomic DNA NOT useful for isoforms?

Introns still present → doesn’t reflect final protein

What causes muscle depolarization at NMJ?

Na⁺ influx

Does Ca²⁺ cause depolarization?

No → Ca²⁺ causes contraction, not depolarization

• Ovarian cells

• Skin (epidermis)

• Alveoli (lungs)

• GI tract lining (stomach, intestines)

• Kidney tubules

• Endocrine glands (thyroid, pituitary)

• Exocrine glands (sweat, salivary)

epithelial cells (lines things, secretes/hormones/enzymes, absorbs nutrients)

exocrine glands -

sweat, salivary

endocrine glands -

thyroid, pituitary

• Bone cells (osteoclasts, osteoblasts)

• Cartilage

• Adipose (fat)

• Tendons & ligaments

• Bone marrow

connective tissues - blood, bone, cartilage

nervous tissue compromises:

brain, spinal cord, peripheral nerves, neurons

If a process requires phosphorylation, what inhibits it?

Phosphatase

What activates contraction in VSM?

Ca²⁺ → calmodulin → MLCK → phosphorylates myosin → contraction

If a receptor is NOT expressed in tissue, what happens?

no effect in that tissue

If acetate suppresses insulin signaling in WT but not knockout, what does that mean?

Effect is receptor-dependent (GPR43-dependent)

Rate-limiting enzyme of pentose phosphate pathway

what does pentose phosphate pathway produce?

NADPH + Ribose-5-phosphate

If enzyme activity increases, what happens to products?

Products ↑, substrate ↓

Succinyl-CoA synthetase produces what?

succinate + GTP

Where are protons pumped?

Matrix → intermembrane space

If gradient dissipates, what decreases?

Protons in intermembrane space

What does increased membrane permeability do?

Destroys proton gradient

Why use siRNA controls?

• Confirm knockdown works

• Ensure specificity

• Rule out off-target effects

What is a non-specific siRNA control?

Shows effects are NOT due to random interference

Pyruvate → Acetyl-CoA requires what cofactor?

lipoic acid

If mtKAS is inhibited → lipoic acid ↓ → what happens?

↓ Pyruvate dehydrogenase activity

Which molecules can be used for gluconeogenesis?

Lactate, Glycerol, Glucogenic amino acids

Which molecules CANNOT be used for gluconeogenesis?

aceytyl coa and Even-chain fatty acids

Why can’t acetyl-CoA make glucose?

Carbons are lost as CO₂ in TCA → no net glucose production

What is the fastest way the body increases blood glucose?

Glycogenolysis

What pathway is used after glycogen stores are depleted?

Gluconeogenesis

Key enzyme that releases free glucose into blood?

Glucose-6-phosphatase

What enzyme breaks down glycogen?

Glycogen phosphorylase

What activates a G-protein?

GDP → GTP exchange

What does hexokinase do?

Phosphorylates glucose → traps it in the cell