Scott Chapter 12.1 to 12.5: Amino Acids, Peptides, & Proteins Flashcards
Physical properties of some small carboxylic acids
Compared to other organic compounds with similar molecular weight, carboxylic acids have a relatively ____ boiling point due to their ability to form ________ bonds with one another.
High boiling point
Hydrogen Bonds
<em>i.e. Hexan 65°, Hexanoic Acid 205°</em>
Physical properties of some small carboxylic acids
What gives small carboxylic acids a significant water solubility?
The ability to form hydrogen bonds, in addition to the presence of polar C=O, C-O, and O-H bonds, gives small carboxylic acids a significant water solubility.
<em>i.e. once the tail gets too long it deflects water and becomes less soluble as a result. </em>
Carboxylic Acids are Weak Organic Acids
Ka = ………………. = 1.8 x 10-5
Small # = __________
Small # = weak organic acid
Carboxylic Acids are Weak Organic Acids
pH 7 =
Physiological pH
Carboxylic Acids are Weak Organic Acids
Physiological pH =
Carboxylic Acids are Weak Organic Acids
pH 7
Amines
Amines are classified based on what?
Number of Carbon atoms directly attached to the nitrogen atom
1°, 2°, 3°, 4°
Amines
Amines are ______ of one another.
What type of bonding takes place in 1°, 2°, and 3° amines?
Isomers
1° = H-Bonding (strong IMF)
2° = H-Bonding (strong IMF)
3° = No H-Bonding (Bp drops due to no IMF holding together. <u>More soluble</u>)
Amines
___° and ___° amines form hydrogen bonds with like amines.
___° amines do not form hydrogen bonds with each other.
1° and 2°
3°
Amines as Weak Organic Bases
Amines _____ H+ from water.
Amines _____ H+ from acid.
accept
accept
Amino Acids
Describe the structure of amino acids and the system used to classify amino acids.
Amino acids are molecules that contain at least one caboxyl (CO2H) group and one amino group (NH2).
Amino acids are classified into four different types based on the nature of their side chain. (side chain determines solubility)
Amino Acids
Distinguish between oligopeptides, polypeptides, and proteins.
Length: A polypeptide is a single linear chain of many amino acids, held together by amide bonds. A protein consists of one or more polypeptides (more than about 50 amino acids long). An oligopeptide consists of only a few amino acids(between two and twenty).
Amino Acids
In a protein, amino acid residues are connected to one another through a _________.
Peptide Bond
also called amide bond
Amino Acids
The end of the peptide chain with the unreacted amino group is called the _______.
The end of the peptide chain with the amino group that’s modified to an amide is called the _______.
N-terminus (left)
C-terminus (right)
Amino Acids
What is chymotrypsin?
A Digestive Enzyme
Amino Acids
Peptides and proteins are named by listing the amino acid residue, in order, from the __________ to the ___________.
N-terminus to the C-terminus
Amino Acids
In terms of peptides and proteins, define primary structures.
Name the covalent and noncovalent forces.
The order of amino acid residues in a peptide or protein is referred to as its primary structure.
same letters diff meanings: edit, diet, tide, tied
H-Bonding
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Amino Acids
In terms of peptides and proteins, define secondary structures.
Name the covalent and noncovalent forces.
The properties of proteins depend not only on their sequence of amino acid residues but also on how they are folded and twisted.
H-Bonding
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Amino Acids
In terms of peptides and proteins, define tertiary structures.
Name the covalent an noncovalent forces.
The overall three-dimensional shape of a protein is referred to as its tertiary structure.
H-Bonding, Salt Bridges, Disulfide Bonds, Londons Forces
Amino Acids
The conformation in the tertiary structure that leads to a biologically active protein is called ________.
Tertiary structures sometimes include nonpeptide components called ________.
a native conformation
Prosthetic groups
Amino Acids
Proteins that require a prosthetic group for biological activity are called ____ and those without are called _____.
(not made of amino acids)
Complex
Simple
(not made of amino acids)
Amino Acids
In terms of peptides and proteins, define quaternary structures.
Name the covalent and noncovalent forces.
Cooperation between subunits is a factor in regulation of _______.
Require more than one polypeptide chain to be biologically active. Quaternary structure refers to the arrangement of these chains.
H-Bonding, Londons, Salt Bridges
Protein activity. (hands working together to peal orange)
Amino Acids
Any change of protein conformation caused by disruption on noncovalent forces and disulfide bridges responsible for maintaining native conformation is called _________
Denaturation
Amino Acids
List some ways to denature a protein.
Heat
Changes in pH
Agitation
Denaturing agents (soap/detergent)
Amino Acids
What is the solubility rule for proteins that maximizes its interaction with water
nonpolar in, polar out
Amino Acids
The arrangement of multiple polypeptide chains in a functioning protein is called the ________ structure of the protein.
Quaternary
Amino Acids
A major structural protein found in tendons, cartilage and bones is called
Collagen
Amino Acids
Prosthetic groups are nonpeptide components tightly bound to a polypeptide chain. What is the name of the prosthetic group in hemoglobin?
Heme
Amino Acids
The form of the amino acid that has one positive and one negative charge is called a (an)
Zwitterion
Amino Acids
Polar Basic vs Polar Acidic vs Polar Neutral
Polar Basic contains an amid (O=C–NH2)
Polar Acidic contains carboxylate ion (O=C–O-)
Polar Neutral contains zwitterions (+)(-)
Describe the quaternary structure of hemoglobin. The binding of oxygen to hemoglobin is cooperative. Explain this term.
A single hemoglobin molecule is a tetramer consisting of four separate polypeptide chains, two identical alpha chains two identical beta chains. Each alpha and beta chain carries a heme prosthetic group.
In molecules with multiple binding sites binding is said to be cooperative if binding at one site impacts the binding at other sites. Hemoglobin has four oxygen binding sites. The binding of oxygen to any one subunit leads to change in shape at three other sites or subunits which increases its ability to bind to oxygen.