Chapter 3: 3.2 Protein Structure Flashcards
What are amino acids comprised of?
- A basic amino group (-NH2)
- Acidic carboxyl group (-COOH)
- A hydrogen (H)
- A side chain (-R) attached to an α-carbon
How are peptide bonds formed? What type of bonds are they?
Created from the reaction of a carboxyl group of one amino acid to the amino group of a second amino acid
* This is a covalent bond
There are – essential amino acids
- 20
What determines what group an amino acid belongs to?
The side chain (at pH 7.0)
List
The 20 amino acids
- Glycine (G) (Gly)
- Alanine (A) (Ala)
- Valine (V) (Val)
- Leucine (L) (Leu)
- Isoleucine (I) (Ile)
- Methionine (M) (Met)
- Phenylalanine (F) (Phe)
- Tryptophan (W) (Trp)
- Proline (P) (Pro)
- Serine (S) (Ser)
- Threonine (T) (Thr)
- Cysteine (C) (Cys)
- Tyrosine (Y) (Tyr)
- Asparagine (N) (Asn)
- Glutamine (Q) (Gln)
- Aspartate (D) (Asp)
- Glutamate (E) (Glu)
- Lysine (K) (Lys)
- Arginine (R) (Arg)
- Histidine (H) (His)
Which amino acids have nonpolar side chains?
- Glycine
- Alanine
- Valine
- Leucine
- Isoleucine
- Methionine
- Phenylalanine
- Tryptophan
- Proline
Which amino acids have polar side chains?
- Serine
- Threonine
- Cysteine
- Tyrosine
- Asparagine
- Glutamine
Which amino acids have electrically charged side chains?
Acidic
1. Aspartate
2. Glutamate
Basic
1. Lysine
2. Arginine
3. Histidine
The ——– group of one amino acid binds to the —– group of an adjacent amino acid forming a ——- bond
- Carboxyl
- Amino
- Peptide
Define:
Primary Structure
The sequence of amino acids in a chain
In primary structure:
How is the protein sequence written?
In N to C direction
* One end has an amino group (NH2)
* One has a carboxyl group (COOH) left open
Define:
Secondary Structure
Refers to the conformation of the protein as a result of hydrogen bonds between the carbonyl oxygen and the hydrogen of the amino group of amino acids within the primary structure
What can secondary structure be like?
- α-helix
- β-pleated sheet
Define:
Tertiary Structure
Refers to the 3-D shape of the protein as it curls and folds as a result of bonding between R-groups
What forces contribute to the tertiary structure? (5)
- Disulphide bonds between two cysteine residues
- Ionic interactions
- Hydrogen bonds
- van der Waals forces
- The Hydrophobic effect
Define:
Quaternary Structure
Refers to the binding of two or more polypeptide chains together
True or False:
Quaternary structures form by non-covalent interactions
True
Compare:
Hydrophobic group vs. Hydrophilic group
- Hydrophobic group: Ones that don’t bind well with water
- Hydrophilic group: Bind to water well through H-bonds
Describe:
Hydrophobic amino acids
- Generally non-polar (hydrocarbons)
- No electronegative molecules to create a permanent dipole needed to H-bond with water
Describe:
Hydrophilic amino acids
- Generally polar
- Electronegative N or O to create permanent dipoles and H-bond with water
Describe:
Globular proteins
Fold so that:
* Hydrophobic groups are buried in the interior core
* Hydrophilic groups remain on the surface where they can interact with water
Describe:
Membrane spanning proteins
- Have a hydrophobic domain within membrane
- Have a hydrophilic domain on the extracellular and intracellular surfaces
What is protein denaturation?
Temperatures above a certain threshold (melting temperature or Tm) cause proteins to unfold due to breaking of non-covalent bonds
In protein denaturation:
Tertiary structure goes to what structure in denaturing?
Primary structure