CHEM 103 Final Exam UKY |Questions and Answers
Polypeptide - -sequence of amino acids b/w 10 and 100 in length.
-Protein - -is a peptide that is greater than 100 amino acids in length.
-Three Dimensional - -The __________ ___________ structure of a protein is critical to its
function.
-4 - -There are ____ levels that a structure can be broken down into.
-Primary Structure - -- is the amino acid sequence of a protein
- peptide bonds form the connections b/w the amino acids.
- read from the N-terminus (free amino group) to the
C-terminus (free carboxyl group).
-Secondary Structure - -- ordered patterns of 3D arrangements on localized regions of the
BACKBONE
- Two main types of proteins: Alpha Helix and Beta Pleated Sheets.
- secondary structures are stabilized by extensive hydrogen bonding between the side
chains.
- Hydrogen bond b/w carbonyl oxygens (C = O) and amide nitrogens (N - H)
-Alpha Helix - -consists of amino acids that adopt a spiral shape
-Beta Pleated Sheets - -is alternating rows of amino acids
that line up in a side-by-side fashion. (like fan folded paper)
-Tertiary Structure (Globular) - -- overall 3D structure of a protein
- stabilized by attractive intermolecular forces such as : London forces, hydrogen bonding,
dipole-dipole forces, ion-dipole interactions, ionic salt bridges, and disulfide
bonds
- interactions b/w and among secondary structures
-Quaternary Structure - -- multiple protein subunits
- specific interaction and orientation of the subunits of that protein
- i.e. hemoglobin contains 4 subunits (2 alpha subunits and 2 beta subunits)
- these hemoglobin subunits come together through interactions of subchains.
-Globular - -Many types of proteins are __________
-Keratin, fibrous - -_________ proteins are _________ and make up the skin, nails, and outer
layer of skin
-Denaturation - -____________ is any change in
, the three-dimensional structure of a protein that renders it incapable of performing its
assigned function
-Primary - -denaturation occurs in all structures BUT ___________.
-Heat, organic compounds, pH, and heavy metal ions - -Factors such as ________, __________
___________, ______ , and _________ __________ ________ can cause protein denaturation
-Globular proteins - -The delicately folded __________ __________ are much easier to denature
than are the tough, fibrous proteins of hair and skin.
-Amino Acids - -- the building blocks of proteins
- contain carboxylic acid group (COOH-) and amino group (H2N)
-Proton Donor - -A carboxylic acid is the ________ ________.
-Proton Acceptor - -The basic amino group is the _______ ________.
-Alpha Carbon - -the carbon in the middle is know as the _______ ________.
-20 - -How many different amino acids found in proteins are there?
-Side chains, R group - -The 20 different amino acids differ in their _______ _______, which we
call ____ _________.
-Positive and negative - -When an amino acid contains both a __________ and _________ charge
but NO net charge, we call that a zwitterion (backbone).
-aqueous - -The zwitterion is commonly found in _________ solutions.
-pH - -The overall charge of an amino acid is dependent upon the ______ of the solution.
-Isoelectric Point - -Neutral pH is also known as the ____________ _________.
-H+ - -In an ACIDIC solution you have an excess of ______ ions.
-OH- - -In a BASIC solution you have an excess of ______ ions.
-pH < pI - -
-pH > pI - -
-zwitterion - -
-glutamate and asparate - -What are the only 2 acidic amino acids in the 20?
Polypeptide - -sequence of amino acids b/w 10 and 100 in length.
-Protein - -is a peptide that is greater than 100 amino acids in length.
-Three Dimensional - -The __________ ___________ structure of a protein is critical to its
function.
-4 - -There are ____ levels that a structure can be broken down into.
-Primary Structure - -- is the amino acid sequence of a protein
- peptide bonds form the connections b/w the amino acids.
- read from the N-terminus (free amino group) to the
C-terminus (free carboxyl group).
-Secondary Structure - -- ordered patterns of 3D arrangements on localized regions of the
BACKBONE
- Two main types of proteins: Alpha Helix and Beta Pleated Sheets.
- secondary structures are stabilized by extensive hydrogen bonding between the side
chains.
- Hydrogen bond b/w carbonyl oxygens (C = O) and amide nitrogens (N - H)
-Alpha Helix - -consists of amino acids that adopt a spiral shape
-Beta Pleated Sheets - -is alternating rows of amino acids
that line up in a side-by-side fashion. (like fan folded paper)
-Tertiary Structure (Globular) - -- overall 3D structure of a protein
- stabilized by attractive intermolecular forces such as : London forces, hydrogen bonding,
dipole-dipole forces, ion-dipole interactions, ionic salt bridges, and disulfide
bonds
- interactions b/w and among secondary structures
-Quaternary Structure - -- multiple protein subunits
- specific interaction and orientation of the subunits of that protein
- i.e. hemoglobin contains 4 subunits (2 alpha subunits and 2 beta subunits)
- these hemoglobin subunits come together through interactions of subchains.
-Globular - -Many types of proteins are __________
-Keratin, fibrous - -_________ proteins are _________ and make up the skin, nails, and outer
layer of skin
-Denaturation - -____________ is any change in
, the three-dimensional structure of a protein that renders it incapable of performing its
assigned function
-Primary - -denaturation occurs in all structures BUT ___________.
-Heat, organic compounds, pH, and heavy metal ions - -Factors such as ________, __________
___________, ______ , and _________ __________ ________ can cause protein denaturation
-Globular proteins - -The delicately folded __________ __________ are much easier to denature
than are the tough, fibrous proteins of hair and skin.
-Amino Acids - -- the building blocks of proteins
- contain carboxylic acid group (COOH-) and amino group (H2N)
-Proton Donor - -A carboxylic acid is the ________ ________.
-Proton Acceptor - -The basic amino group is the _______ ________.
-Alpha Carbon - -the carbon in the middle is know as the _______ ________.
-20 - -How many different amino acids found in proteins are there?
-Side chains, R group - -The 20 different amino acids differ in their _______ _______, which we
call ____ _________.
-Positive and negative - -When an amino acid contains both a __________ and _________ charge
but NO net charge, we call that a zwitterion (backbone).
-aqueous - -The zwitterion is commonly found in _________ solutions.
-pH - -The overall charge of an amino acid is dependent upon the ______ of the solution.
-Isoelectric Point - -Neutral pH is also known as the ____________ _________.
-H+ - -In an ACIDIC solution you have an excess of ______ ions.
-OH- - -In a BASIC solution you have an excess of ______ ions.
-pH < pI - -
-pH > pI - -
-zwitterion - -
-glutamate and asparate - -What are the only 2 acidic amino acids in the 20?
