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95 Cards in this Set

  • Front
  • Back
Proteins are molecules that controls every human activity including
1. digestion
2. buildup of body muscles
3. movement
4. helps breathing transport of oxygen
Proteins _____ contain the genetic code
Proteins do not contain the genetic code
Proteins are made of amino acid and the nature and function of a protein is dependent upon how the amino acids is arranged in a _____ (i.e.) the sequence of the amino acid arrangement.
Proteins are made of amino acid and the nature and function of a protein is dependent upon how the amino acids is arranged in a protein molecule (i.e.) the sequence of the amino acid arrangement.
Proteins are not an energy source only about ___% of human energy is derived from a protein.
Proteins are not an energy source only about 10% of human energy is derived from a protein.
Out of 100s of amino acids, only ___ amino acids, participate in making a protein.
Out of 100s of amino acids, only 20 amino acids, participate in making a protein.
What is the molecular weight of proteins?
40 MM proteins
Amino acids exist as _____ (i.e.) contain positive and negative charge
Amino acids exist as zwitter ions (i.e.) contain positive and negative charge
Amino acids are _____ (i.e.) contain both an acid and a base
Amino acids are amphoteric molecules (i.e.) contain both an acid and a base
All the 20 amino acids are the same except the _____
All the 20 amino acids are the same except the "R" side chain
Types of amino acids
1. neutral nonpolar (9)
2. neutral polar (6)
3. acidic amino acids (2)
4. basic amino acids (3)
The net charge of an amino acid is _____
zero
The pH, which is the amino acid, have a net charge of zero it is _____
isoelectric point (PI)
At a pH less than the PI (isoelectric point), the net charge of an amino acid is _____
(+1)
At a pH higher than the PH (isoelectric point), the net charge of an amino acid is _____
(-1)
Essential Amino Acids
• only obtained from diet (e.g. meat, eggs, milk, soy products)
• not synthesized in humans
• proteins that provide all the essential amino acids are known as complete or adequate proteins. Diet that lacks are in complete proteins.
Corn does not contain
TRP and LYS
Nonessential Amino Acids
• synthesized in humans from the essential amino acids which are obtained from the diet
Rice contains _____ & _____ but not _____
Rice contains MET & TRP but not LYSINE
Beans contain _____
lysine
Rice + Beans →
complementary proteins
Amino acids combine together to lose water to result in amide known as _____
Amino acids combine together to lose water to result in amide known as peptides
"N" terminis
is always at the left end of the peptide
"C" terminis
is always at the right end
2 amino acids is a ______
dipeptide
3 amino acids is a _____
tripeptide
4-10 amino acids is a _____
oligopeptide
11-49 amino acids is a _____
polypeptide
50 & ↑ amino acids is a _____
protein
_____ or _____ produced in the brain
appetite enhancing peptide → obesity peptide
Neuropeptide y or galantine produced in the brain appetite enhancing peptide → obesity peptide
_____ is an appetite inhibiting peptide
Cholecystakonin is an appetite inhibiting peptide
_____ is a 9 amino acid oligopeptide regulates blood pressure
Vasopressin is a 9 amino acid oligopeptide regulates blood pressure
Oxytocin (Pytocin) is a 9 amino acid oligopeptide produced in the uterus
1. enhancing or stimulates the uterus contraction during childbirth
2. stimulate mammary gland during lactation
3. enhances maternal characteristics
Vasopressing and oxytocin are produced in the
pituitary glands
Feel good or pain relieving peptides are _____ and _____
Met-enkhaphalin and Leu-enkhaphalin (natural endorphins)
Structure of Met-enkhaphalin
TYR.GLY.PHE.PHE.MET
Structure of Leu-enkhaphalin
TYR.GLY.PHE.PHE.LEU
A pain enhancing peptide is
Bradykinin (9 amino acid oligopeptide)
What are globular proteins?
• enzymes are globular proteins
• helps digest food of the diet
What are structural proteins?
• Fibrous proteins (ex: nail, hair, hooves, & skin contain keratinized)
What are defense proteins?
• prevents blood clot in the arteries and thus prevent athlerosclerosis
• interferon - defends the immune system
• snake venom
What are transport proteins?
• hemoglobin transports oxygen
• lipoproteins

LDL, HDL, and VLDL are all transport cholesterol triglycerides
What are movement proteins?
• muscles, tissues, help etc.
What are structural proteins?
• bone, skin, cartilage, tendon & collagen is skin
What are storage proteins?
• casein in milk
• egg yolk
What are stress response proteins?
• cytochome (check page 450)
• metallothionein → "cysteinerich metallothionein"
What are the different structures of proteins?
• primary structure
• secondary structure
• tertiary structure
• quarternary structure
• Allosteric Protein structure
Primary Structure
means or reveals that amino acid sequence of arrangement is a protein. The function and the nature of the protein is dependent on how the amino acid are arranged. The sequence of the amino acid arrangement can not be mutated or altered. Even a small alteration will drastically affect the function of a protein.

E.g. hemoglobin, a protein present in the blood is made of four biologically active peptide molecules
Oxygen carrier
VAL.HIS.LEU.THR.PRO.GLU.GLU.LYS

oxygen carrier
Sickle cell carrier
VAL.HIS.LEU.THR.PRO.VAL.GLU.LYS

sickle cell carrier
One change in an amino acid alters the _____ of the protein
One change in an amino acid alters the function of the protein
Insulin is made up of peptide molecule chain
A (21 amino acids) & B (30 amino acids)
INSULIN
Chains A & B are intermolecularly connected by two disulfide linkages between two _____ amino acids
INSULIN
Chains A & B are intermolecularly connected by two disulfide linkages between two cysteine amino acids
Chain A of insulin contains an intermolecular ____ linkage
Chain A of insulin contains an intermolecular disulfide linkage
_____ is essential for metabolizing glucose
Insulin is essential for metabolizing glucose
Type ___ diabetes is due to absence or inability to produce insulin
Type 1 diabetes is due to absence or inability to produce insulin
Type ___ diabetes is due to inadequate protection of biosynthetic insulin and; it is a "lifestyle disease"
Type 2 diabetes is due to inadequate protection of biosynthetic insulin and; it is a "lifestyle disease"
Ingestion of insulin inhibits _____ insulin
Ingestion of insulin inhibits biosynthetic insulin
What is the source of insulin?
traditionally harvested from animal pancreas currently obtained genetic engineered insulin
What is myoglobin?
a 153 amino acid, single strand protein GLY .... GLY carries O₂ to the muscles tissues and stores in the muscles and helps endurance
What is the structure of oxytocin?
AAAAA
Secondary Structure of Proteins
refers to the spatial arrangement of amino within the primary structure (i.e. hydrogen bonding) within the primary structure
What are the three kinds of secondary structures?
1. alpha helix
2. B pleated
3. Triple helix
alpha (α) helix
proteins like nails, hair, hooves, collagen, keratin contain alpha helix structure

• a single strand protein is coiled like a rod with right handed confirmation containing hydrogen bonding between hydrogen of the amino group and the oxygen of the carbonyl group (C=O) of amino acids remotely, This results in the strength of the above proteins
β pleated
• fibroin and silk
• two or more strands of biologically active peptide molecules arranged side by side. Fully extended (not coiled) like a ladder containing collinear hydrogen bonding between the amino acids parallel β-pleated (i.e. arranged in the same order)

(i.e. coliner hydrogen increases the anti-parallel β-pleated)
Triple helix
• present in cartilage, tendon, bone, etc
• 3 strands of proteins are coiled or woven like a braid
Tertiary Structures of Proteins refers to
refers to the 3-dimensional conformations assumed by proteins; and this known as native configuration or natural confirmation. The natural and function of a protein depends upon the side chain interactions of various amino acids in the single strand proteins the chain interactions
TERTIARY STRUCTURES OF PROTEINS
_____ interaction is the interaction between the neutral nonpolar groups
Hydrophobic interaction is the interaction between the neutral nonpolar groups
TERTIARY STRUCTURES OF PROTEINS
_____ interaction: interaction between neutral polar [OH] groups
Hydrophobic interaction: interaction between neutral polar [OH] groups
TERTIARY STRUCTURES OF PROTEINS
_____ bonding interaction between neutral polar groups
Hydrogen bonding interaction between neutral polar groups
TERTIARY STRUCTURES OF PROTEINS
_____ or _____ or electrostatic interaction
Ionic or salt bridge or electrostatic interaction
TERTIARY STRUCTURES OF PROTEINS

LYS .... LYS
Disulfide linkage or covalent bonding
Disulfide linkage or covalent bonding
Tertiary Structure (i.e.) R-group interaction in a single strand proteins occur in between the amino acids: and it is present in globular proteins known and "enzyme" (i.e.) intramolecular R-group interactions are present in the enzymes
Tertiary Structure (i.e.) R-group interaction in a single strand proteins occur in between the amino acids: and it is present in globular proteins known and "enzyme" (i.e.) intramolecular R-group interactions are present in the enzymes
Quarternary Structures of proteins contain the same ....... present in the tertiary structures.
1. hydrophobic
2. hydrophilic
3. hydrogen bonding
4. electrostatic
The side chain interactions in the quaternary structures are intermolecular (i.e.) ...
the R-group interact in between the peptide molecules
Quarternary structures are present in the ____ proteins (i.e.)
Quarternary structures are present in the oligo proteins (i.e.) proteins containing two or more biologically active proteins molecules
Hemoglobin
an O₂ carrier contains four biologically active peptide molecules and hence exhibit a quaternary structure
denaturation or destruction of the active proteins
If proteins are subjected to two conditions that would destroy the side chain interactions present in the tertiary & quaternary protein structures and the hydrogen bonding
Denaturation of proteins does not affect the _____ structure
Denaturation of proteins does not affect the primary structure
Heat destroys the _____ and _____ bonding
Heat destroys the hydrophobic & hydrogen bonding
Alcohol destroys _____ and _____ but not water
Alcohol destroys hydrogen bonding and hydrophobic interaction but not water
Strong acids and bases destroy the ionic and hydrogen bonding salt bridge
Strong acids and bases destroy the _____ and _____ _____ _____ ____
Mechanical stress destroys the _____
Mechanical stress destroys the hydrophobic interaction
Heavy metals including Ag, Pb, and Hg destroy the _____ _____ and _____ _____.
Heavy metals including Ag, Pb, and Hg destroy the ionic bonding and disulfide linkage.
Disulfides are produced by _____ [reducing agent]
Disulfides are produced by Mercaptoethanol [reducing agent]
What are vitamins?
• water soluble "coenzymes"
• water insoluble "health food"
What are enzymes?
are known as biological catalysts; that increase the biochemical reactions in the tissue cells by reducing the activation energy
lactose →(lactase)
β-d-galactose & α-d-glucose
sucrose →(sucrase)
β-d-fructose & α-d-glucose
triglycerides →(lipase)
glycerol & fatty acids
protein →1. pepsin 2. trypsin
amino acids
Enzymes are very specific in the activity; and the substrate binds to a site known as the "_____ _____" thru their side chain interactions and them metabolizes
Enzymes are very specific in the activity; and the substrate binds to a site known as the "active site" thru their side chain interactions and them metabolizes
The shape of the active site of an enzyme is the _____ the substrate so they can bind effectively.
The shape of the active site of an enzyme is the same as the substrate so they can bind effectively.
The shapes of the active site of an enzyme and the substrate is like a "____ ____ ____" model
The shapes of the active site of an enzyme and the substrate is like a "lock and key" model
The lock and key model is known as a ______
fixed model
In certain cases: Induced fit model enzymes adjust their shape to accommodate the substrate and the substrate in turn adjusts its shape to fit into the active site, and when the biochemical reactions are complete both enzymes and substrates regain the original shape.
In certain cases: Induced fit model enzymes adjust their shape to accommodate the substrate and the substrate in turn adjusts its shape to fit into the active site, and when the biochemical reactions are complete both enzymes and substrates regain the original shape.