genetic quiz 1 finals Flashcards by Jasmine Tabangcora

which the sequence of codons within
mRNA provides the information

traslation

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Synthesis of proteins in ribosomes

translatiion

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as an adapter molecule that
carries the amino acids

tRNA

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Are composed of one or more polypeptides

protein

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Genes
that encode the amino acid sequence of polypeptide.

Protein-encoding genes (Structural genes)-

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Most COMMON ORGANIC MOLECULE in the body

amino acid

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an acid (can donate a proton)

A carboxyl group (COOH)`

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a base (can accept a proton)

An amino group (NH2):

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Unique structure of R-
group dictates the function of the amino acid in the protein

A distinctive side chain (R-group):

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Most of the amino acids are

α-amino acids

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It means both amino and carboxyl groups are attached to
the α-carbon atom

α-amino acids

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neither carboxyl group nor amino
group is attached to the α-carbon atom

non-α-amino acids

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all amino acids in human proteins

L-configuration:

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bacterial cell walls, antibiotics

D-configuration:

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refers to an amino acid which bear NO NET CHARGE
at the isoelectric pH (pI)

Zwitterionm

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Carboxyl group is dissociated or deprotonated →

COO-

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Amino group is protonated →

NH3+

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Has the smallest side chain; only achiral amino acid among the 20
AAs

glycine

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Carrier of ammonia and of the carbons of pyruvate from skeletal muscle
to liver (Site of ammonia disposal)

ALANINE

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Disrupts the alpha-helix structure of proteins

glycine

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Together with glycine, constitutes a major fraction of free amino acids in
the blood

ALANINE

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Branched-chain amino acids whose metabolites accumulate in maple
syrup urine disease

VALINE, LEUCINE, ISOLEUCINE

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Accumulates in phenylketonuria (Mousy odor)

PHENYLALANINE

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Precursor of tyrosine

PHENYLALANINE

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Has the LARGEST SIDE CHAIN

TRYPTOPHAN

Precursor for niacin, serotonin, and melatonin

TRYPTOPHAN

Precursor of homocysteine and cysteine

METHIONINE

Not an amino, but an IMINO ACID

PROLINE

* Tyrosine is the precursor of several compounds:

Phenylalanine → Tyrosine → L-dopa → Dopamine →Norepinephrine → Epinephrine

is the site for N-linked glycosylation of proteins

Asparagine

is deaminated by glutaminase resulting in the formation of ammonia, and is a major carrier of nitrogen to the liver from peripheral tissues

Glutamine

Contains a sulfhydryl group that is an active part of many enzymes

CYSTEINE

Two cysteines can be connected by a covalent disulfide bond to form

CYSTEINE

ACIDIC AMINIO ACIDS (serve as PROTON DONORS)

ASPARTATE, GLUTAMATE

is the precursor for GABA and glutathione

Glutamate

BASIC AMINIO ACIDS (serve as PROTON ACCEPTOR)

HISTIDINE, ARGININE, LYSINE

Arginine and lysine are positively charged Histidine, being a weak base, has no charge

Precursor of histamine

HISTIDINE

Precursor of creatinine, urea, citrulline, and nitric oxide

ARGININE

Precursor of carnitine

LYSINE

Found in a handful of proteins, including certain peroxidases and reductases, where it participates in the catalysis of electron transfer reactions

SELENOCYCSTEINE

*Known to be present in archaea from a methanogenic lineage (Methanosarcinales), found in the GI tract of humans

PYRROLYSINE

Refers to amino acids which cannot be synthesized in the body; hence they are ESSENTIAL IN DIET

ESSENTIAL

Refers to amino acids which can be synthesized in the body; hence they are NON-ESSENTIAL IN DIET

NON-ESSENTIAL

Refers to amino acids which are required in growing children, but not essential in adults

SEMI-ESSENTIAL

MOST ABUNDANT and functionally diverse molecules in living systems

PROTEIN

* Monomers: Amino acids * Polymers: Proteins

Determined by the amino acid sequence of a protein

PRIMARY STRUCTURE

attach the α-amino group of one amino to the α- carbonyl group of another

Peptide bonds

Proteins are naturally synthesized from the N-terminus (NH3 end) to the C-terminus (COOH end)

N-TERMINUS AND C-TERMINUS

Contains targeting signals (targets protein to a specific organelle)

N-terminus

Contains retention signals for protein sorting (keeps the protein in the endoplasmic reticulum)

C-terminus

Stabilized by hydrogen bonding

SECONDARY STRUCTURE

Most common secondary structure

ALPHA HELIX

Spiral structure with polypeptide backbone core, with side chains extending outward

ALPHA HELIX

Amino acid residues form a zigzag or pleated pattern

BETA SHEET

R groups of adjacent residues project in opposite directions

BETA SHEET

Supersecondary structures produced by packing side chains from adjacent secondary structural elements close to each other

MOTIFS

Overall, 3-dimensional shape of the protein

MOTIFS

Fundamental functional and three-dimensional structural units of polypeptide

DOMAINS

Number and types of polypeptide units of oligomeric proteins and their spatial arrangement

QUATERNARY STRUCTURE

Specialized group of proteins required for the proper folding of many species of proteins

CHAPERONES

Prevent aggregation,

CHAPERONES

Can also “rescue” proteins that have become thermodynamically trapped in a misfolded dead end by unfolding hydrophobic regions

CHAPERONES

unfolding and disorganization of the protein’s secondary and tertiary structures

DENATURATION

Spherical in shape

GLOBULAR PROTEINS

More soluble

GLOBULAR PROTEINS

Has DYNAMIC functions

GLOBULAR PROTEINS

Heme protein found exclusively in red blood cells (RBCs)

Hemoglobin

low oxygen affinity

T (taut) form

high oxygen affinity (300x)

R (relaxed) form

Heme protein present in heart and skeletal muscle

Myoglobin

can be detected in plasma following a myocardial infarction

Myoglobin

Reservoir of oxygen * Oxygen carrier that increases the rate of transport of O2 within the muscle cell

Myoglobin

ELONGATED or NEEDLE in shape

FIBROUS PROTEINS

Minimal soluble

FIBROUS PROTEINS

Has STRUCTURAL proteins

FIBROUS PROTEINS

Most abundant protein in the body

Collagen

Most common form of this collage is

type 1 collagen

Rich in glycine and proline

collagen

Formed in fibroblasts (or in the osteoblasts of bone and chondroblasts of cartilage)

Collagen

BONE, skin, tendon, dentin, fascia, cornea, LATE wound repair

TYPE 1

CARTILAGE (including hyaline), vitreous body, nucleus pulposus

TYPE 2

RETRICULIN, skin, blood vessels, uterus, fetal tissue, granulation tissue (EARLY wound repair)

Type 3

BASEMENT MEMBRANE or basal lamina

TYPE 4

ANCHORING FIBRILS- found beneath the stratified squamous epithelium

TYPE 7

Connective tissue protein with rubber-like

elastin

genetic quiz 1 finals Flashcards

(87 cards)