Proteins Flashcards
is an amino acid in which the amino group, the carboxyl group and the hydrogen atom are attached to the a-carbon atom
a-amino acid
All amino acids are alpha-amino acids except _____ which is an imino acid.
Proline
is an amino acid that contains one amino group, one carboxyl group, and a nonpolar side chain.
Nonpolar amino acid
is an amino acid that contains one amino group, one carboxyl group, and a side chain that is polar but neutral.
Polar neutral
is an amino acid that contains two amino groups and one carboxyl group, the second amino group being part of the side chain
Polar basic
is an amino acid that contains one amino group and two carboxyl groups, the second carboxyl group being part of the side chain
Polar acidic
CLASSIFICATION OF AMINO ACIDS:
G,A,V,L,I,P,F,M,W
Nonpolar amino acid
CLASSIFICATION OF AMINO ACIDS:
S,C,N,T,Q,Y
Polar neutral
CLASSIFICATION OF AMINO ACIDS:
H,K,R
Polar basic
CLASSIFICATION OF AMINO ACIDS:
D,E
Polar acidic
CLASSIFICATION OF AMINO ACIDS:
D,E
Polar acidic
a standard amino acid needed for protein synthesis that must be obtained from dietary sources because the human body cannot synthesize it in adequate amount.
ESSENTIAL AMINO ACIDS
Synthesized by the body.
NON-ESSENTIAL AMINO ACIDS
ESSENTIAL OR NON-ESSENTIAL AMINO ACIDS:
R*,H,M,I,L,K,W,T,F,V
ESSENTIAL AMINO ACIDS
ESSENTIAL OR NON-ESSENTIAL AMINO ACIDS:
C,A,N,D,E,Y,S, Q,G,P
NON-ESSENTIAL AMINO ACIDS
is a protein that contains all of the essential amino acids in the same relative amounts in which the body needs them. This may or may not contain all of the nonessential amino acids
COMPLETE DIETARY PROTEIN
is a protein that does not contain adequate amounts, relative to the body’s needs, of one or more of the essential amino acids
INCOMPLETE DIETARY PROTEIN
is an essential amino acid that is missing, or present in inadequate amounts, in an incomplete dietary protein
LIMITING AMINO ACID
are two or more incomplete dietary proteins that, when combined, provide an adequate amount of all essential amino acids relative to the body’s needs. Ex. Rice and beans servings.
COMPLEMENTARY DIETARY PROTEINS
Necessary for the synthesis of neurotransmitter serotonin (5-hydroxytryptamine). A natural relaxant, helps alleviate insomnia by inducing normal sleep; reduces anxiety and depression
Tryptophan
Can be metabolized to niacin Vit. B3 if needed
Tryptophan
Used to synthesized melatonin (5-methoxy-N-acetyltryptamine)
Tryptophan
Precursor of dopamine, norepinephrine, epinephrine
Promotes healthy thyroid functioning
Tyrosine
enhance energy, increase endurance, and aid in muscle tissue recovery and repair.
Valine, Isoleucine, Leucine
lowers elevated blood sugar levels and increases growth hormone production
Valine, Isoleucine, Leucine
precursor for L-carathine which is essential for healthy nervous system function.
Lysine
for adequate absorption of calcium and bone development in children
Lysine
Is antioxidant. It helps in breakdown of fats and aids in reducing muscle degeneration. Helps lower cholesterol levels by increasing the liver’s production of lecithin; reduces liver fat and protects the kidneys
Methionine
principle supplier of sulfur, which inactivates free radicals. Is a natural chelating agent for heavy metals and helps detoxify the body of these metals
Methionine
Adequate ______ prevents disorders of the hair, skin and nails
Methionine
Beneficial for healthy nervous system. It may be useful against depression and suppressing appetite
Phenylalanine
Used to produce dopamine and norepinephrine, chemicals that promote alertness, elevate mood, decrease pain, aid in memory and learning, and reduce hunger and appetite
Phenylalanine
Type of Phenylalanine:
natural form. May improve rigidity, walking disabilities, speech difficulties and depression associated with Parkinson’s disease
D-phenylalanine
Type of Phenylalanine:
can be converted into L-tyrosine, which is in turn converted into L-DOPA. L-DOPA is a precursor for dopamine, norepinephrine (noradrenalin), and epinephrine (adrenaline)
L-phenylalanine
Removes toxic substances released from breakdown of muscle protein during intensive exercise
Alanine
antioxidant (free radical scavenger), and has synergetic effect when taken with other antioxidants such as vitamin E and selenium.
Cysteine
Promotes healthy brain function. It is also necessary for the synthesis of RNA and DNA molecules.
Glutamine
Component of skin and is beneficial for wound healing. It acts as neurotransmitter
Glycine
Important for the synthesis of red and white blood cells.
Histidine
It is a precursor for histamine which is good for sexual arousal. Improve blood flow.
Histidine
It helps promote equilibrium in the central nervous system—aids in balancing state of emotion.
Threonine
Enhances stamina, aids in removal of toxins and ammonia from the body, and beneficial in the synthesis of proteins involved in the immune system.
Aspartic Acid
plays role in intracellular signaling.
Proline
plays role in blood vessel relaxation, stimulating and maintaining erection in men, production of ejaculate, and removal of excess ammonia from the body.
Arginine
Is a molecule that has a positive charge on one atom and a negative charge on another atom, but which has no net charge.
Zwitterion
It is the pH at which an amino acid exists primarily in its zwitterion form.
Isoelectric Point
formed by a biochemical reaction that extracts a water(H2O) molecule as it joins the amino group of one amino acid to the carboxyl group of a neighboring amino acid.
Peptide Bonds
is a covalent bond between the carboxyl group of one amino acid and the amino group of another amino acid
Peptide Bonds
The linear sequence of amino acids within a protein is considered the _______ of the protein.
Primary Structure
Proteins are built from a set of only _____ amino acids
Twenty (20)
The largest group of amino acids have _______ side chains
Nonpolar
Hydrophobic side chains interact with each other via __________
weak van der Waals interactions.
TYPES OF PEPTIDE BOND:
w/ 2 or more amino acids
Dipeptide
TYPES OF PEPTIDE BOND:
w/ 3 or more amino acids joined together in a chain
Tripeptide
TYPES OF PEPTIDE BOND:
w/ 10 or 20 amino acid residues are present in a chain
oligopeptide
TYPES OF PEPTIDE BOND:
w/ longer unbranched chain of amino acids
Polypeptide
Uterus-Contracting Hormone
(also stimulates lactation)
Oxytocin
Enhances reabsorption of free water and plays a role in Blood pressure control
Vasopression (ADH or antidiuretic hormone)
pain killers
neuromodulators in the brain and spinal cord; involved with pain perception, movement, mood, behavior, and neuroendocrine regulation
Enkephalins
Found in most living cells as antioxidant & promote tissue growth
Glutathione
(governs release of thyrotropin) or TSH or thyroid-stimulating hormone
TRH (Thyrotropin Releasing Hormone)
Pressor Agent. Can increase blood pressure by vasoconstriction.; can also trigger thirst or the desire for salt. Is responsible for the release of the pituitary gland’s ADH
Angiotensin II
Inhibits Growth Hormone Release (used to treat ulcers)
Somatostatin
Hypotensive Vasodilator (acts on smooth muscle)
Bradykinin
Potent Vasoconstrictor (structurally similar to some
snake venoms)
Endothelin
Honey Bee Venom (used to treat rheumatism)
Mellitin
Hyperglycemic Factor (used as an anti-diabetic)
Glucagon
Pancreatic Hormone (used in treatment of diabetes)
Insulin
amino acid sequence — drives the folding and intramolecular bonding of the linear amino acid chain, which ultimately determines the protein’s unique three-dimensional shape
primary structure
Hydrogen bonding between amino groups and carboxyl groups in neighboring regions of the protein chain sometimes causes certain patterns of folding to occur. Known as alpha helices and beta sheets, these stable folding patterns make up the _____________ of a protein
secondary structure
The ensemble of formations and folds in a single linear chain of amino acids — sometimes called a polypeptide — constitutes the _______ of a protein.
tertiary structure
refers to those macromolecules with multiple polypeptide chains or subunits.
quaternary structure
It is the hydrogen bonding of the peptide hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern.
Secondary structure
It includes three-dimensional folding pattern or a protein due to side chain interactions
Tertiary structure
It is the protein consisting of more than one amino acid chain.
Quaternary Structure
