Ch. 3 Flashcards
What is an Organic Molecule?
Molecules that contain Carbon.
Example: Glucose (C6H12O6)
What is an Inorganic Molecule?
Do not contain Carbon.
Example: Water (H2O)
What is a Hydrocarbon?
A molecule that contains one Carbon and Hydrogen.
Example: Methane (CH4)
Even charge distribution (Non-polar)
What are Function Groups?
The C-H backbone and specific groups of many organic molecules.
What does it mean when molecules have similar functional groups?
They often have similar properties.
What are some common functional groups?
- OH Hydroxyl Group
- C=O Carbonyl Group
- COOH Carboxyl Group
- PO4 Phosphate Group
- NH2 Amine Group
What are Polymers?
Large aggregates of smaller sub-units.
Can be thought of as long trains that are made by linking together many individuals.
What are monomers?
The individual sub-units that make up a polymer.
What are 4 main types of macromolecules?
Proteins
Nucleic Acids
Lipids
Carbohydrates
What are 2 types of proteins?
Globular and structural
What is the sub-unit of proteins?
Amino Acids
What are the functions and examples of proteins?
Enzymes (Hemoglobin) and support (Keratin, Collagen)
What are 2 types of Nucleic Acids?
DNA and RNA
What is the sub-unit of Nucleic Acids?
Nucleotides
What are the function and example of Nucleic Acids?
Gene coding (Chromosomes) and Gene Expression (mRNA).
What are 3 types and sub-units of lipids?
Fats (Glycerol, 3 fatty acids)
Phospholipids (Glycerol, 2 fatty acids)
Steroids (Carbon rings)
What are the Function and example of each type of lipid?
Fats (Energy storage; Butter, Olive Oil)
Phospholipids (Cell Membranes; Lipid Bilayer)
Steroids (Hormones; Estrogen)
What are 3 types of Carbohydrates and their sub-units?
Starch (Glucose, simple sugar)
Cellulose (Glucose, simple sugar)
Chitins (Modified glucose)
What are the function and examples of each of the 3 types of carbohydrates?
Starch (Energy storage; potatoes)
Cellulose (Cell walls (plants); celery strings)
Chitins (Structural; Crab shells)
What does Dehydration Synthesis do?
Used to build macromolecules. An -OH from one molecule and an H+ from another are removed and the sub-units are joined.
Cells expend energy to assemble the macromolecules.
What is Hydrolysis?
The breakdown of macromolecules by breaking the bonds by adding an -H to one end and a -OH to the other.
-Lysis means break
What are six functions of proteins?
- Enzyme Catalysis
- Defense
- Transport
- Support
- Motion
- Regulation
What is an example of Enzyme Catalysis?
-Help to speed up chemical reactions.
What is an example of protein defense?
Globular proteins attach to foreign molecules forming the basis for the immune system.
What is an example of protein transport?
Hemoglobin transporting Oxygen in the bloodstream.
What are examples of protein support?
- Fibrous, structural proteins help keep us together.
- Keratin makes hair
- Fibrin makes blood clots
- Collagen makes skin, ligament, cartilage, and bones
What is an example of protein motion?
Actin and Myosin are contractile proteins that are responsible for moving materials in cells and the motion of muscles.
What is an example of protein regulation?
Some hormones are small proteins that are used to send messages between cells. These turn on and off certain genes are used to regulate growth, development, etc.
What groups are proteins comprised of?
All amino acids have an amine group, a carboxyl group and a side group {R}.
In amino acids, what does the R group determine?
The chemical properties.
How many common amino acids are there, and how many classes?
20 common amino acids, and they are broken into 5 classes of R groups.
What are the 5 classes of R Groups?
Non-polar amino acids; R groups with -CH2 or -CH3
-Example: Alanine, Valine
-These are hydrophobic
Polar, uncharged amino acids; R groups contain Oxygen
-Example: Glutamine
-These are hydrophilic
Ionizable amino acids; R groups contain acids or bases
-Example: Glutamic acid
-These are hydrophilic
Aromatic amino acids; R groups contain benzene ring
-Example: Phenylalanine
Special amino acids
-Methionine, first amino acid in polypeptide
-Proline, causes kinks in protein chains
-Cysteine, bonds with itself to bend protein
How do amino acids join together?
By undergoing condensation (dehydration synthesis)
What are peptide bonds?
The bond between two amino acids.
It isn’t a flexible bond which allows for the protein to maintain a tight shape which in turn determines function for many proteins.
What are polypeptides?
Give an example.
Long chains of amino acids joined together by peptide bonds.
Example: hemoglobin is comprised of 4 polypeptide chains.
What amino acids tend to be on the surface of the protein?
Charged, polar amino acids.
In a protein, how many levels of structure are there, and what are they?
- 6 levels of structure
- Primary (Amino Acid Sequence), Secondary (Coils and sheets), Motifs (Combinations of secondary), Tertiary (3-D shape), Domains (Exons), & Quaternary (Arrangement of polypeptide chains)
What is the primary structure of proteins?
The specific amino acid sequence
- Determined by the nucleotide sequence of the gene that codes for the protein.
- A protein can consist of any amino acid sequence since the R groups aren’t involved in the peptide bonds.
If a polypeptide is 100 amino acids long, how many possible combinations are there?
20^100 possible combinations.
What is the secondary structure of proteins?
The folding of the polypeptide chain into the characteristic shapes.
The -COOH and the -NH3 ends can form hydrogen bonds with each other
- The hydrogen bonds causes patterns in the protein shape.
- Alpha helix (a-helix); looks like a spring
- Beta pleated sheet (B-pleated sheet); looks like a curled up sheet.
What is the motif level of structure of proteins?
Combinations of secondary structure.
-Also called super secondary structure.
What is the tertiary structure of proteins?
The final folded shape of the protein (3D shape).
- Hydrophobic interaction help determine the tertiary structure.
- Chemical nature of the side groups {R-Groups} helps to determine the final shape.
- The different size of the R-groups of the non-polar amino acids allow for a very exact fit. Helps to keep the final shape of the protein very stable.
- Disulfide bonds between Cysteine (R-Group= CH2SH)
What are Van Der Waal’s forces?
Weak intra-atomic forces caused by the slight change in polarity of atoms as the electrons move about the nucleus of the atoms.
-Affects the tertiary structure of proteins.
What are domains of a protein?
- Contain exons (functional unit)
- A single polypeptide chain consists of several linked domains.
- Domains have independent functions:
* One domain will bind to a cofactor
* Another will help bind to substrate
What are exons?
- Genes encoded in functional sectionals.
- Exons are typically 100 to 200 amino acids long and fold into a structurally independent unit.
What are the quaternary structure of a protein?
Arrangement of polypeptide chains
-Each polypeptide chain is a sub-unit of the quaternary structure.
Example: Hemoglobin is made of 4 chains (2 alpha chains, and 2 beta chains)
-Interfaces between sub-units are often non-polar amino acids that help hold the protein together.
What are chaperonins?
About how many kinds are there?
Special proteins that help in the assembly of other proteins.
About 17 kinds
-Thought to work by fixing proteins that are incorrectly folded.
What diseases may be linked to Chaperonin deficiencies?
Cystic fibrosis and Alzheimer’s disease