WGU C785
Terms in this set (263)
What is the basic structure amino group (NH2 or NH3), carboxyl group (COO or
of an amino acid? What do COOH), alpha carbon (C), and variable group
they look like?
How do you identify the 3 Non-polar/hydrophobic - end with CH or "can't have"
different types of side water. Polar - end with OH, SH, or NH. Charged - end
chains: non- with a charge
polar/hydrophobic, polar,
and charged?
what kinds of bonds do ionic, hydrophobic/non-polar, charged
each of the 3 different
types of side chains make?
Primary - linear structure, Secondary - Folded into helix
or pleated sheet caused by hydrogen bonding, tertiary -
What are the 4 levels of
3D structure caused by side chain interactions,
protein structure?
quaternary - 1+ amino acid chains combine = multiple
subunits MUST have 1+ subunit
hydrophobic - temperature change, ionic - salt or
What enviormental change
decreased pH, hydrogen - temperature, change in pH,
breaks each type of bond?
disulfide - reducing agents
what type of amino acid hydrophobic bonds
side chain leads to protein
aggregration?
how do environmental Extreme temp can cause hydrogen bonds to break apart
changes affect protein = malformation of protein folding
folding?
how do mutations affect Can cause structure to change. Protein loses form =
protein structure? loses function. May form a different protein.
, What is an electron? Negatively charged atom on outer ring for bonding
What is energy: Power derived fro chemical interaction
what are covalent bonds? chemical bond, atoms share 1+ valence electrons
what is an ionic bond? bond between positive and negative
what is a hydrogen bond? weak bond between positive and negative
with an amino? piece of amino acid, NH2 or NH3
what is a carboyxl? piece of amino acid, COO or COOH
What is hydrophobic? Doesn't like water, end with CH
what is hydrophilic? Water Lovering, end with OH, NH, or SH
strongest bond between reduction agents, formed
what is disulfide bond?
between SH's.
amino with positive and negative charges = overall
what are zwitterions?
charge of zero
what is a polypeptide polymer of amino acids
What is dehydration Process of forming peptide bonds
synthesis?
what is hydrolysis? adding water to destroy bonds
what is an alpha helix? twisted secondary structure, formed by hydrogen bonds
folded second structure shape, formed by hydrogen
what is a beta sheet?
bonds
loss of shape duet o interruption of chemical bonds;
what is denaturation?
occurs via extreme salt, temp, pH
clumping of inner or outer cellular proteins caused by
what is aggregation? misfolded proteins leading to diseases such as
Alzheimers, ALS, Parkinson's
how do enzymes catalyze bind with substrates to decrease activation energy
reactions? required and decrease reaction rate
Terms in this set (263)
What is the basic structure amino group (NH2 or NH3), carboxyl group (COO or
of an amino acid? What do COOH), alpha carbon (C), and variable group
they look like?
How do you identify the 3 Non-polar/hydrophobic - end with CH or "can't have"
different types of side water. Polar - end with OH, SH, or NH. Charged - end
chains: non- with a charge
polar/hydrophobic, polar,
and charged?
what kinds of bonds do ionic, hydrophobic/non-polar, charged
each of the 3 different
types of side chains make?
Primary - linear structure, Secondary - Folded into helix
or pleated sheet caused by hydrogen bonding, tertiary -
What are the 4 levels of
3D structure caused by side chain interactions,
protein structure?
quaternary - 1+ amino acid chains combine = multiple
subunits MUST have 1+ subunit
hydrophobic - temperature change, ionic - salt or
What enviormental change
decreased pH, hydrogen - temperature, change in pH,
breaks each type of bond?
disulfide - reducing agents
what type of amino acid hydrophobic bonds
side chain leads to protein
aggregration?
how do environmental Extreme temp can cause hydrogen bonds to break apart
changes affect protein = malformation of protein folding
folding?
how do mutations affect Can cause structure to change. Protein loses form =
protein structure? loses function. May form a different protein.
, What is an electron? Negatively charged atom on outer ring for bonding
What is energy: Power derived fro chemical interaction
what are covalent bonds? chemical bond, atoms share 1+ valence electrons
what is an ionic bond? bond between positive and negative
what is a hydrogen bond? weak bond between positive and negative
with an amino? piece of amino acid, NH2 or NH3
what is a carboyxl? piece of amino acid, COO or COOH
What is hydrophobic? Doesn't like water, end with CH
what is hydrophilic? Water Lovering, end with OH, NH, or SH
strongest bond between reduction agents, formed
what is disulfide bond?
between SH's.
amino with positive and negative charges = overall
what are zwitterions?
charge of zero
what is a polypeptide polymer of amino acids
What is dehydration Process of forming peptide bonds
synthesis?
what is hydrolysis? adding water to destroy bonds
what is an alpha helix? twisted secondary structure, formed by hydrogen bonds
folded second structure shape, formed by hydrogen
what is a beta sheet?
bonds
loss of shape duet o interruption of chemical bonds;
what is denaturation?
occurs via extreme salt, temp, pH
clumping of inner or outer cellular proteins caused by
what is aggregation? misfolded proteins leading to diseases such as
Alzheimers, ALS, Parkinson's
how do enzymes catalyze bind with substrates to decrease activation energy
reactions? required and decrease reaction rate
