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H3N C C
O
H
The
zwitterionic form of
an amino acid
R1
H3N C C
O
H
R1
H H
H +
O
H NCC
O
H
H
H3N C C N C C
O
R2
H O
=
R2
H2O
both the H atom and R groups are opposite of the carbonyl O atom to avoid steric
clash
amino acid polymers of less than 50 amino acids are often called peptides though
there is no strict cut off between the terms peptide and protein
the Carbon of each amino acid can always be recognized since the R group
is attached
the peptide bond occurs between the carbonyl group of the first amino acid and the
amine group of the next amino acid
Identify the Carbon and the Side chain (R group) of each amino acid in this
five amino acid peptide.
Locate each peptide bond in the peptide.
Note that every peptide or protein begins with the amino group of the first
amino acid and ends with the carboxyl group of the last amino acid.
Thus we refer to the start of a protein as the Amino terminus or N-terminus
and the end of a protein as the Carboxyl terminus or C-terminus
Planar
Rigid
free to
rotate
But, proteins have a very complex and convoluted structure and this is due to
the bonds that can rotate somewhat freely
free to
rotate
free to
rotate
Planar
Rigid
The bonds before and after the peptide bond can rotate
these are the bonds that flank the alpha Carbon of each amino acid
peptide bonds
peptide bonds
The phi and psi bonds have rotational freedom, but not unlimited freedom
Permissible
Not Permissible
=-180o, =+180o
=-0o, =+180o
=-180o, =+0o
Nelson p144
Nelson p103
because of the permissible phi and psi bond angles within amino acids,
the polypeptide or protein backbone can form a (not unlimited) range of
conformations.
due to the combination of possible bond angles coupled with Hydrogen bonding
effects, certain amino acid segments spontaneously form secondary structures
some proteins are made up of only -helices or only -sheets while others are
mixtures of both secondary structure types. Loops and turns often connect
helices or sheets together.
VDGQFEQKKKQKDETYDIEHLIACFSPMIRKKLSNTSYQEREDLEQELKIKMFEKADMLLCQDVPGFWEFILYMVDENS
N
Primary sequence and predicted secondary structure of a small 79 amino acid protein
Many Beta strands can associate in mixed orientations to form beta sheets
stabilized by intra-molecular H bonding
Anti-parallel arrangement
Parallel arrangement
Proline and Glycine often participate in forming turns (nearly 180o change in direction
of polypeptide backbone)
Proline at either one of
these positions will mediate
a Turn
Ala
Pro
Nelson p175
VDGQFEQKKKQKDETYDIEHLIACFSPMIRKKLSNTSYQEREDLEQELKIKMFEKADMLLCQDVPGFWEFILYMVDENS
C
Primary sequence and predicted secondary structure of a small 79 amino acid protein
homodimers
homotrimers
homotetramers
etc.
Nelson p183
This Lecture
Stryer 8th Chapter 2 Protein Composition and Structure pg 27-57
Next Lecture
Stryer 8th Chapter 3 Exploring Proteins and Proteomes pg 66-79