Unit 1 Biochemistry Flashcards
What are the four main types of biological macromolecules?
*carbohydrates
*lipids
*proteins
*nucleic acid
What is a lipid?
A nonpolar organic compound (normally consist of hydrogen, nitrogen, small amount of oxygen)
4 functions of lipids in humans
- long term energy storage
- insulated internal organs
- membrane structure (phospholipids)
- system-wide message molecules (hormones)
5 categories of lipids
- Fatty acid
- Fats
- Phospholipid
- Steroids
- Waxes
Fatty acid is a hydrocarbon chain with what fuctional group at the end?
Carboxyl groups (carboxylic acid)
What did the carboxyl group do to the properties of the fatty acid?
How does the length of the HC chain affect this property?
- COOH makes it slightly soluable
- increase in length of the CH chain, decease in the solubity
2 types of fatty acid and their sturture
- Saturated fatty acid: all hydrocarbons chain with single bond
- Unsatruated fatty acid: hydrocarbon chains that conatin double or triple bond
What is a name of a unsaturated fatty acid with 2 or more double bonds?
Provide 2 exapmles
polyunsaturated fatty acid
(e.g omega 3, omega 6)
What is the shape of unsaturated and saturated fatty acid?
- saturated: linear
- unsatrurated: bent or linear
What is a bent unsatrurated fatty acid called?
cic fatty acid
What is a linear unsatrurated fatty acid called?
trans fatty acid
What is the name of the process of turning an unsaturated fat into a saturated fat by adding hydrogens?
And what do we call those fatty acids?
- hydrogenation
- hydrogenated
Fat is made from condensation of which two product?
glycerol and up to 3 fatty acids
What is name of the linking that connects the glycerol and the fatty acid into a fat molecule? Which part (atoms) are involved?
ester linkage (COC=O)
What is the name of the fat made with glycerol and one fatty acid?
monoglyceride
What is the name of the fat made with glycerol and two fatty acid?
diglyceride
What is the name of the fat made with glycerol and three fatty acid?
triglyceride
Fat that only consisted at saturated fatty acid are called ___________ (also describe their state and why it cause the state)
saturated fat (solid in room temperature, by strong IMF’s)
Fat that contain one or more unsaturated at saturated fatty acid are called ___________ (also describe their state and why it cause the state)
unsaturated fat (liquid in room temperature, weaker IMF as bent prevent alignment)
What are the most unhealthy fat? (also describe their state and why it cause the state)
trans unsaturated fat (solid in room temperature, linear, densely stack together, strong IMFs)
Two types of fat that insulate our bodies from high/low temperature
*subcutaneous fat: fat found under the skin
*visceral fat: fat found deep within a body and surrounding organs
What is called when a molecule contains both a polar and a non-polar region? (e.g. phospholipids)
amphipathic
What is a steroid?
A lipid with a base framework of 4 carbon rings
What are the two types of cholesterol
*high density lipoprotein (good cholesterol): picks up the cholesterol in our body and send to to the liver for removal
*low density lipoprotein (bad cholesterol): can build up in artery walls
What is a molecule released into the fluid tissues of an organism that helps regulate its growth or behavior called?
hormones
What are non natural steroids called?
anabolic steroids
What are waxes?
A large lipid, formed by the bonding of fatty acids to OH and carbon ring
What are the characteristics of waxes?
*non-polar
*soft solid
What is the main function of a nucleic acid?
serve as an instruction for proteins production
What are the two types of nucleic acid and chemical formula
DNA (deoxyribonucleic acid) C5 H10 O4
RNA (ribonucleic acid) C5 H10 O5
What the monomer of a nucleic acid called? and it’s composition
nucleotide (phosphate group, pentose sugar ring, nitrogenous base)
What is a nucleoside?
molecule with only a pentose sugar ring and a nitrogenous ring
The two types of nitrogenous base and their structure
pyrimidines (1 ringed), purines (2 ringed)
3 types of pyrimidines
cytosine, thymine, uracil
2 types of purines
adenine, guanine
What the name of the bond between two nucleotide and it’s chemical formula
phosphodiester bond (COPCO)
Which two Carbon molecule does the phosphodiester bond forms?
C3 and C5 (bonded phosphate group)
What is the different structure of DNA and RNA
RNA: single-stranded
DNA: double-stranded, double helix structure
How is the two strand of DNA bonded together?
Hydrogen bond between nitrogenous bond of the two strands
How many H bond is form between the two set pairs of nucleobase?
A-T: 2 H-bond
G-C: 3 H-bond
How is the two DNA strands organized?
antiparallel (one have a C3 end and one have a C5 phosphate end)
Which 4 nucleobase does DNA and RNA has?
DNA: AT,CG
RNA: AU-CG
\What makes nucleic acid acidic?
The donation of H+ ions in the phosphate group to water molecules
Which carbon is the phosphate group and the nucleobase bonded to?
PO4: C5
Nucleobase: C1
What are the 7 functions of proteins?
- Structural proteins
- Defensive Proteins
- Signal proteins
- Receptor proteins
- Carrier proteins
- Enzymes
- Motile Proteins
What is the formation structure of an amino acid?
central carbon bonded with an amino group, carboxyl group, hydrogen and R group
What are those amino acid that cannot be produce by human body called? How many of those?
essential amino acid, 9 types
What are those amino acid that can be produce by human body called? How many of those?
non-essential amino acid, 11 types
What are called when an amino acid is bonded in a chain? What is called when the chain is really long?
peptides, polypeptides
What is the name of the bonds between amino acid?
peptide bonds
What are the side with C, COOH, NH2 on the peptide chain called?
backbone
What are the side with R groups called in a peptide chain?
side group
What are the four steps of protein production (names only)?
- Primary Structure
- Secondary Structure
- Tertiary Structure
- Quaternary Structure
What happens in the primary structure of a protein?
A unique linear structure of amino acid in peptide bonds
2 types of secondary structure, What happens in the secondary structure of a protein?
- alpha helix: H-bond on the 4th amino acid on the backbone
*beta pleated: H-bond between backbone side-by-side (each strand about 3-10 amino acid long)
What happens in the tertiary structure of a protein?
Folding and coiling due to the interactions of R groups:
4 types of interactions:
*H-bond
*hydrophobic interactions (LDFs)
*disulfide bridges (covalent)
*ionic bond
What happens in the quaternary structure of a protein?
*Combination of two or more tertiary proteins, head together by interactions of R groups in each
*Each polypeptide chain are called subunit
What is the molecule that is not a protein that could added in in the quaternary structure for function?
proteins prosthetic groups
What are the two common types of structure of a protein? And where are they found in a human body?
*Fibrous Protein: long, linear (found in muscle, silk and hair)
*Globular Protein: contain sites that a specific molecule can bind to (found in enzymes, receptors, carrier proteins)
What is the process of protein losing it’s structure called? Why does it occur?
Protein denature: Cause by proteins being subjected to hard conditions (e.g. heat, radiation, acidic) or mutation
What is the reverse process of protein denature?
Protein renature
What is the compound that speeds up reaction called? And what is the name of energy required for a reaction?
catalysts, activation energy
What is called when a chemical reaction releases energy?
exothermic reaction
What is called when a chemical reaction absorb energy?
endothermic reaction
What is the molecule that an enzymes act upon called?
substrate
What is a Induced-fit?
An enzymes changes it conformation after the substrate enter the activation site
The two chemical structure (sites) of an enzymes
active site, allosteric site
What is the combination of an enzymes and a substrate in a temporary state called?
enzymes-substrate complex
What are two types of inhibitor of enzymes?
competitive inhibitor, allosteric inhibitor
How does competition inhibitor works?
The inhibitor attaches to the active site, preventing any substrate from binding
How does allosteric inhibitor works?
The inhibitor is a regulatory molecule binds to a allosteric site, changes the shape of the active site and the enzymes become inactive.
Some enzymes are normally inactive unless an ____________ binds to its allosteric site
allosteric activator
Some inhibitors are _________ and the enzyme can be turned on and off. Other times, an inhibitor may permanently ________ or _________ an enzyme.
temporary, deactivate, denature
