Bio/Biochem NEW

Zwitterion

molecule that contains charges but is neutral overall

Isoelectric focusing

Method of separating proteins using their isoelectric points by electrophoresis

Electrophoresis

Separating compounds by size and charge using an electric field; protein uses polyacrylamide and nucleic acid uses agarose

Centrifugatioin

Separating components based on density by spinning them; most dense form solid and least dense remain in liquid

Bradford protein assay

colorimetric method of determining protein concentration by comparing to standard

Lyase

enzyme that cleaves or synthesizes molecule without using water

Peptide Bond

Amide bond between carboxyl group and amino group of two amino acids

Zymogen

Enzyme secreted in inactive form and must be activated by cleavage

Uncompetitive inhibition

Decrease in enzyme activity by binding to enzyme-substrate complex causing it to be unable to release; increase affinity and decreases velocity

Saturation of fatty acids

Saturated only have single bonds, while unsaturated have at least one double bond

Mixed inhibition

Decrease in enzymatic activity caused by inhibitors that bind to enzyme and enzyme bound substrate

Ligase

Enzyme that joins large polymers together

Kinase

specific transferase enzyme that moves phosphate group

Holoenzyme

Active enzyme bound with coenzyme of cofactor

Cofactor

Inorganic molecule or ion that helps stabilize enzyme

Coenzyme

organic molecule that helps enzyme carry biochemical reactions

Apoenzyme

Enzyme with no coenzyme or cofactor

Tertiary protein structure

Interactions between R groups

Isoelectric point

pH at which an amino acid is in it’s neutral form

Lower than isoelectric point

Positively charged

Higher than isoelectric point

Negatively charged

Cooperation

Interactions between subunits of a protein in which binding increases affinity and vice versa

Conjugated protein

Protein that contains a prosthetic group

Prosthetic Group

cofactor or coenzyme covalently bonded to a protein to permit function

Positively charged amino acids

Arginine, lysine, histidine

Negatively charged amino acids

Aspartic acid and glutamic acid

Amino acids with sulfur

Cysteine and methionine

Aromatic amino acids

Phenylalanine, tryptophan, and tyrosine

Amino acids that can be phosphorylated

Tyrosine, threonine, and serine

Wobble Hypothesis

Third base of a codon is less strict and allows a single tRNA to recognize multiple codons; theorized to protect against mutations

Transcription factors

Regulate gene expression by helping RNA polymerasae II locate and bind to promoter

Spliceosome

Splices out introns and brings exons together during mRNA processing

Shine-Dalgarno Sequence

Site of translation initiation in prokaryotes

Ribozyme

RNA molecule with enzymatic activity; can catalyze biochemical reactions

Release factor

Protein that binds to the stop codon during translation termination

Promoter region

Contains TATA box and is where RNA polymerase binds

Polycistronic

One mRNA codes for multiple proteins

Operator Region

Part of the operon where the repressor can bind

mRNA

RNA formed after transcription; gets moved to the cytoplasm for translation

Lariat

Lasso shaped structure formed during removal of introns

Initiation

Start of translation where ribosome pieces bind to mRNA and tRNA brings first amino acid

Heterochromatin

Tightly coiled DNA that can’t be transcripted

Euchromatin

Loosely bound DNA that can be transcripted

Reverse transcriptase

Enzyme in retroviruses that converts viral RNA into DNA allowing it to integrate into host’s genome

Peroxisome

organelle that has hydrogen peroxide to breakdown fatty acid chains

Obligate intracellular organisms

organisms that need a host to express genes and reproduce

Lytic cycle

Phase in viral replication where host cell is lysed and releases virions

Virions

Infective form of a virus outside host cell

Lysogenic cycle

Phase of viral replication where bacteriophage DNA integrates into host’s genome

Facultative anaerobe

Can use aerobic respiration but doesn’t have to

Conjugation

Joining of bacteria using a bridge to exchange genetic material

Bacteriophages

Virus that only infect bacteria

Eukaryote ribosome subunits

40s and 60s

Prokaryote ribosome subunits

30s and 50s

Enhancer

Part of DNA that can be bound by transcription factors to increase transcription

White fibers

Fast twitch, anaerobic and fatigue fast

Tricuspid valve

Between right atria and right ventrible

Transverse tubules

In muscle and are channels for ions to flow through, such as calcium from SR

Systole

Heart muscle contracts and pumps blood

Diastole

Heart muscle relaxes and allows filling of blood

Surfactant

Liquid produced by lungs and reduces surface tension in alveoli

Where does most digestion occur in small intestine?

Duodenum

Where does most absorption take place in small intestine?

Jejunum and ileum

Semilunar valves

Prevent backflow of blood from arteries into ventricles

Rh factors

Surface protein on RBCs that can induce immune response

Red fiber

Slow twitch fibers that are aerobic and last longer

Pyloric sphincter

Between stomach and small intestine and regulates chyme flow

Proximal convoluted tubule

Where reabsorption of nutrients and organic molecules occurs

What does plasma contain

Majority water and then proteins, salts, nutrients, gases, and hormones

Pepsin

Secreted by chief cells and initiates protein digestion

Respiratory Pathway

Nasal cavity, pharynx, larynx, trachea, bronchi, bronchioles, alveoli

Electrical Impulse of Heart

SA node, AV node, bundle of His, purkinje fibers

Osteoclasts

Cells involved in bone degredation

Osteoblasts

Cells involved in bone formation