Unit 7 Flashcards
Collagen can be classified as a ______ protein
_structural_______
Proteins that stimulate immune response are known as
immunoglobin
Amino acids that are not synthesized in the body but must be ingested with the diet are called ________ amino acids.
essential
A zwitterion of any amino acid has a net charge of
zero
The isoelectric point for any amino acid is the pH at which the amino acid has a net charge of
zero
hemoglobin is a
quaternary transport protien
1) The protein folds into a compact structure stabilized by interactions between R groups
tertiary
2) the combination of two or more protein molecules to form an active protein
quaternary
3) pleated sheet
secondary
4) the peptide bonds between the amino acids
primary structure
5) the structural level achieved when hydrogen bonds form between the carboxyl group of one amino acid and the amino group of a different amino acid
secondary
list all essential amino acids
1) Tryptophan
2) Lysine
3) Methionine
4) Phenylalanine
5) Threonine
6) Valine
7) Leucine
8) Isoleucine
essential amino acid for kids
histadine and arginine
Lysine
abbreviation
Lys, K
Argine Abrev
Arg, R
Methionine Abrev
Met, M
Tyrosine Abrev
Tyr, Y
Glycine Abrev
Gly, G
Alanine Abrev
Ala, A
Valine Abrev
Val, V
Leucine Abrev
Leu, L
Isoleucine Abrev
Ile, I
Phenylaline Abrev
Phe, F
Methionine Abrev
Met, M
Proline Abrev
Pro, P
Tryptophan Abrev
Trp, W
Serine Abrev
Ser, S
Theronine Abrev
Thr, T
Tyrosine Abrev
Tyr, Y
Cysteine Abrev
Cys, C
Asparagine Abrev
Asn, N
Aspartate Abrev
Asp, D
Glutamine Abrev
Gln, Q
Glutamate Abrev
Glu, E
Histidine Abrev
His, H
Lysine Abrev
Lys, K
Arginine Abrev
Arg, R
endings changed
ine or ate to ly
How many different amino acids are present in proteins?
20
Proteins are said to be polymers. True/ False
True. A protein is a polymer constructed from a set of monomers called amino acids.
Explain the general structure of an amino acid. Give an example.
central C atom (alpha) which is attached to NH2 group, COOH group, H atom and “R”.
Define peptide bond.
The amide bond formed when amino acids combine through condensation reaction is known as a peptide bond.
A peptide bond (amide bond) is a covalent chemical bond linking two consecutive amino acid monomers along a peptide or protein chain
- List the types of protein.
1) Enzyme
2) Hormones
3) Storage
4) Transport
5) Contractile
6) Structure
7) Immunity
2 transport proteins
hemoglobin
cytochromes
2 hormone proteins
insulin
renin
2 structure proteins
collagen
keratin
2 immunity proteins
immunoglobulins
interleukin 4
2 storage proteins
ferritin
casein
a. the sequence of amino acids held by covalent peptide bonds, which is unique for each protein.
primary structure
a. When amino acids form H bonds between atoms and within chains constitute this structure. 2 main types are alpha and beta form. In an alpha helix the amino acids are arranged in a right-handed helical form.
secondary structure
a. The protein folds into a compact structure stabilized by interactions between R groups in this structure. Attractions and repulsions between amino acid residues in polypeptide chain lead to this structure. Most proteins require 2 or more tertiary structures to be biologically active.
tertiary structure
what are the two interactions involved in tertiary structure
hydrophilic
hydrophobic
interactions between external aqueous environment and polar amino acid residues. (remnants of amino acids during the formation of peptide bonds are called residues)
hydrophilic
interactions lead to the formation of a nonpolar region in the center of protein molecule and repelled by hydrophilic interactions.
hydrophobic
ionic attractions between charges of acidic and basic amino acid residues.
salt bridges
bonds formed between H and O or N.
hydrogen bonds
are covalent bonds formed when SH groups are oxidized.
disulfide bonds
a. The combination of two or more protein molecules to form an active protein takes place in this structure
quaternary structure
Combination of 2 or more protein polypeptide chains stabilized by the interactions (discussed in tertiary) constitute this structure. Amino acids with different sequences of alpha and beta chains form similar tertiary structures
quaternary structure
Formed within the same protein chain. Hydrogen bonding can occur between the α-carboxyl group of one residue and the –NH group of its neighbor four units down the same chain. The helical structure can be easily disturbed since hydrogen bond is unstable.
alpha helix
within the same protein molecule consists of two or more amino acid sequences that are arranged adjacently and in parallel, but with alternating orientation. Thus hydrogen bonds can form between the two strands. Hydrogen bonds established between the N-H groups in the backbone of one strand with the C=O groups in the backbone of the adjacent, parallel strand(s). The sheet’s stability and structural rigidity and integrity are the result of multiple such hydrogen bonds arranged in this way.
beta pleated sheet
Which are the protein structures affected by denaturation?
Denaturing disrupts the secondary, tertiary, or quaternary structure of a protein.
Acids and bases denature a protein by
disrupting ionic bonds and hydrogen bonds
An acid can denature a protein by
disrupting hydrogen bonds between R group chains.
Heat denatures a protein by
disrupting hydrophobic bonds and hydrogen bonds.
Heavy metals denature proteins by
disrupting disulfide bonds
One heavy metal that can cause denaturation of a protein is
silver
What are active sites? Where are they found?
The area where the substrates are held are called active sites, found within the enzyme’s tertiary structure.
what happens within active sites
residues of amino acids react with functional groups of substrate to form H bonds, salt bridges and hydrophobic interactions.
Combination of an enzyme and a substrate within the active site forms an
enzyme-substrate complex (ES) that catalyzes the reaction with lower activation energy
R groups on amino acid residues does what
catalyze the reaction to form enzyme-product complex.
(EP) Then the products are
released from the molecule so that it binds with another substrate.
Rate of enzyme-catalyzed reactions are affected by change in
temperature, pH, enzyme and substrate concentration.
Inhibitors decrease enzyme activity by
binding in active site (competitive inhibition) or at another site on the enzyme (noncompetitive inhibition).
Irreversible inhibitor forms a
a covalent bond within the active site that permanently prevents catalytic activity.
Differentiate between enzymes and inhibitors.
Enzymes are the biological catalysts for reactions in our body. Catalyst is a substance which increases the speed of a chemical reaction by choosing another path for the reaction.
Inhibitors decrease enzyme activity by binding in active site (competitive inhibition) or at another site on the enzyme (noncompetitive inhibition). Irreversible inhibitor forms a covalent bond within the active site that permanently prevents catalytic activity.
Proteins are
amino acid chains that fold into unique 3-dimensional structures.
The shape into which a protein naturally folds is known as its
native state, which is determined by its sequence of amino acids and interaction of groups.
The overall charge is zero for the neutral amino acid and is called a
zwitter ion
are considered as the building blocks of proteins.
amino acids
determines the properties of each amino acid because all 3 other groups attached to the alpha C atom are common for all amino acids.
the R group
Due to the presence of a positive amino group and negative carboxyl group, amino acids have properties similar to a
salt
groups H, alkyl and aryl are
non polar
hydrophobic
groups OH, SH, CONH2
polar neutral
hydrophilic
groups COOH
Polar acidic
hydrophilic
Groups NH2
polar basic
hydrophilic
The amide bond formed when amino acids combine through condensation reaction is known as a
peptide bond
When 2 amino acids combine what forms
dipeptide
Proteins are known as polymers due to the presence of
longer chains
The repeating sequence of an amino acid is the
backbone of the dipeptide
The process of breaking larger food molecules down into subunits small enough to diffuse through a cell membrane and to be used by the cell is termed
digestion
catalyzes the digestion of carbs
amylase
catalyzes digestion of proteins
pepsin
helps in emulsifying fats in small intestine.
lipase
These proteins are secreted by endocrine cells to control or regulate biological processes like growth, metabolism, and reproduction.
Hormones
helps in regulating blood glucose levels.
insulin
transports oxygen for use in cellular metabolism
hemoglobin
act as an electron carrier in the electron transport chain.
Cytochromes
in hair, nails and skin helps give these structures strength
keratin
which is a structural protein found in various connective tissues, provides the framework for the ligaments that hold bones together and the tendons that attach muscles to those bones.
collagen
recognize and destroy foreign pathogens in the immune system.
immunoglobulins
helps in muscle contraction and movement. Contractile proteins can cause heart complications if they produce severe contractions.
Actin and Myosin
Storage proteins mainly store
mineral ions such as potassium in your body.
is required for the formation of hemoglobin, the main structural component of red blood cells
Iron
a storage protein, regulates and guards against the adverse effects of excess iron in human body.
Ferritin
Ovalbumin and casein are
are storage proteins found in breast milk and egg whites, respectively, that play a huge role in embryonic development
naturally produced opiates in the body, are found in thalamus and spinal cord tissue. They are polypeptides that have pain-killing properties
Enkephalins
actin and myosin
contractile
lactase and pepsin
enzyme
insulin, oxytocin, somatotropin
hormone
keratin, collagen
structure
ferritin
storage
hemoglobin, cytochromes
transport
elastin, dystrophin
support
immunoglobulin
antibody
