Proteins And Amino Acids Flashcards
(28 cards)
What are sequences of amino acids encoded by?
A gene
How are amino acids classified?
According to chemical properties of the R groups
What determines the acid-base behaviour?
R groups
What are the components of an amino acid?
Amino group
Carboxyl group
H atom
R group
What is a zwitterion? Why is it most common? One property
Net charge of 0 - equal number of positively and negatively charged ions
Most stable
Acts as an acid and a base
Two ends of a polypeptide chain
Amino terminal (NH3+)
Carboxyl terminal (COO-)
What is the acid base behaviour determined by?
The R group
What is an amino acid residue?
Amino acid after it has formed a peptide bond with another amino acid
Chemical properties of R groups
Hydrophobic/philic
Polarity
Acid or Base
What are the two categories of R groups
Aliphatic - only C and H
Aromatic - phenyl ring
What is a peptide bond?
Linking two amino acids
Removing a water molecule
What is an amino terminus and Carboxyl terminus?
+NH3
COO-
What is the shape of a peptide bond and what does it mean?
Planar
On the same plane
What is the central C called?
C alpha
What is a key characteristic of a peptide bond?
What property does this give it?
Partial double bond characteristic between the C and N
Very rigid
Does a peptide have a cis or trans configuration?
Describe it
Nearly always trans
Cs on opposite sides of C-N bond
What are Psi and Phi bonds?
What can they do?
What does this allow?
C alpha - C
C alpha - N
Rotate around the peptide bond
A 3D shape
Define the isoelectric point
The pH at which there is no overall net charge
What stabilises the alpha helix?
H bonds between the N-H and C=O
What is the direction of the alpha helix
Right handed
What are beta sheets composed of?
What is there parallelilty?
What are the bonds?
Adjacent B strands - can be parallel or anti parallel
Stabilised by H bonds between the H on NH and O on C=O
Two comparisons between globular and fibrous proteins
G - compact F - extended
G - several types of secondary structures F - single type of repeating secondary structure
How do polypeptide chains fold in relation to hydrophobic and hydrophilic regions?
Why>
Hydrophobic side chains inside
Charged, hydrophilic regions can interact with aqueous solutions
Describe quaternary structures
Non covalent bonds between complementary hydrophobic and hydrophilic sub units - doesn’t have to be proteins