Lecture 2 Flashcards
3 Attributes Necessary For Life
Infromation, Replication and Storage(IRS)
Parts of an Amino acids
Amino group on one side, carbon in the middle, Carbonyl group on the other side, side chain at the bottom, and H atom at the top
What groups are side chains divided into
Polar, Nonpolar, acidic, and basic
What’s another name for a side chain
R group
Whats another name for amino acids
Residues
How is the solubility of a protein affected by its chemical properties
If the amino acid is charged or polar its hydrophilic and dissolves in water, it the amino acid is uncharged and nonppolar its hydrophobic
How to determine if a an amino acid is polar, nonpolar, acidic, or basic.
- It it is negatively charged, its acidic
- If it is positively charged, its basic
- It it is a neutral charge and it has an oxygen atom its polar
- If it has none of these its nonpolar
Where do you look to determine either something is polar, nonpolar, acidic or baisc
Its R group
peptide bonds
These are created when bonds form between a carbonyl group of one amino acid, and amino group of another
what does polymerize mean?
It means to be created
How does a peptide bond form
It forms through a condensation reaction
What is a condensation reaction?
water is formed
What is a polymer
Its like what the molecules come together to make
what is the polymer of amino acids
Protein
how many types of structures are there in proteins and what are they
Their are 4 types of structures, and these structures are primary, secondary, and tertiary structure.
Primary structure
The sequence of the amino acids
How are the R groups oriented in the primary structure
the R groups stick out of the peptide backbone and interact with each other or water.
What is the Directionality of the sequences
it has ends with N terminus( free amino group) and C Terminus (free carbonyl group) and it usually written with the N terminus first.
What is the flexibilty of the sequences
either terminus can rotate
how many amino acid sequences cna be created?
Over 10,000 billion sequences
How does the shape and sequence of amino acids affect a protein
What a protein does it determined by the shape and sequence of proteins and one change can have a vast effect.
What is secondary structure
The secondary structure is the result of hydrogen bonding and the bonding of one carbonyl group to one of the amino groups
What two shapes result from the secondary structure
alpha helix, and beta pleated sheet
What does a alpha helix look like
It looks like a spring
What doe a beta pleated sheet look like
It looks like two zigzag area’s joined together.
What is a tertiary structure
It is a structure that develops from the interactions of the side chains causing the peptide backbone to bend and fold, creating important 3 dimensional shapes.
How many interactions are there and what are they
There are 5 types of interactions, and they are hydrogen bonding, hydrophobic interactions, Van Der wals interaction, Covalent Bond interaction, and Ionic Bond Interaction
What is a hydrogen bonding Interaction
from between polar side chains and opposite partial charges
What is a hydrophobic interaction
Water forces between hydrophobic side chains( nonpolar side chains)
What is a Van Der Wals interaction?
They are weak electrical interactions between side hydrophobic side chains
Oligopeptide
It is a chain of fewer than 50 aminoacids
Polypetide
Chains of 50 or more amino acids
Covalent bonding Interaction
Covalent bonds bonding between sulfhydryl groups ( Disulfide bonds)
Ioninc Bonding interaction
forms between groups with full and opposing charges
What is a Quaternary stucture?
Bonding of distinct polypeptides
Types of Quaternary Structures:
Dimers, Homedimers, Hetrodimers, Tetramer
What is a dimer
When two polypeptide sub units bond together.
What is a homodimer?
When the structure consists of two identical subunity
What is a heterodimer
When the structure’s sub units are not the same
What is a Tetramer?
when the structure has 4 polypeptide chains
What are moleular chaperones
Molecules that facilitate folding in proteins, they are sesponsible for blocking inappropritate interactions between unfolded proteins
How can folding be described?
It is spontaneous, meaning its due to chemical interactions and usually proteins that are folded are more chemically stable than unfolded proteins
What is a Denatrued Protein:
Unfolded protein
is folding always good.
Altough folding is spontaenous and unfolded proteins dont work properly, folding can be infectious.
What are Prions?
Prions are altered form of proteins and they can induce normal protein molecules to change their shape to the altered form.
What is Kuru and hwo does it relate with prions and infectious protein folding?
Prions that mess up the shape of proteins cause Kuru a disease that was first found in an area where cannibalism is practiced( eating of the brain, which is very high in prions) and these prions cause proteins to have weird shapes(proteins that can make up the nervous system), this results in an attack on a persons nervous system causing them to laugh uncontrollably, have vast emotional mood swings and termors.
