This was a report regarding amino acids and peptides that was prepared by our group and this report made in order to make a score. Hope this slide makes more it to be on help.

1. GROUP 2

2. What is Amino
Acids?
What are
Zwitterions?
Extra steps into
biochemistry
Learning with
molecular models
Table of contents
01
- monomers of proteins
02
You can describe the
topic of the section here
03 04
- mostly electrically neutral
You can describe the
topic of the section here

3. What is Amino
Acids?
01

4. Amino acids are the basic
structural units of proteins consisting of
an amino group, (-NH₂) a carboxyl
(-COOH) group, a hydrogen (H) atom, and a
(variable) distinctive (R) group.
Amino Acids

5. Example of Amino
Acids
Alanine
Serine

6. Each amino acid has a central carbon, called the α-carbon, to
which four different groups are attached.
General Structure

7. Common Amino Acids
Glycine
Proline
Leucine
Cysteine Valine
Serine
Asparagine
Glutamine

8. Classification of amino acids
based on chemical structure
of their side chains
Glycine an amino acid that contains, in its
side chain, only a single hydrogen atom. It is
known to be the simplest amino acid
Cysteine is a naturally occurring,
sulfur-containing amino acid that is
found in most proteins, although only
in small quantities.
Glycine
Cysteine

9. molecules used by all living
things to make proteins
Our body needs 20 different
amino acids to function
correctly
Amino acids usually have a
melting and boiling point that
is very high.
They usually exist in the
form of white, crystalline,
stable compounds.
Some Amino Acid facts
Fact no.1 Fact no.2 Fact no.3
Fact no.4
there are over 500
naturally occurring amino
acids known to us.
only 20 amino acids are
known to appear in genetic
code.
Fact no.5 Fact no.6

11. What are
Zwitterions?
Zwitterions are mostly
electrically neutral
02

12. it is an ion possessing
both positive and
negative electrical
charges.
the pH range in which the
information is required
must be specified
(because a sufficiently
alkaline solution will
change the zwitterion to
an anion, and a
sufficiently acid solution
will change it to a cation).
Zwitterions
The distinction lies in
the fact that the plus
and minus signs on the
amine oxide signify
normal charges.

13.  Amino acids can exist as Enantiomers.

14.  L isomers have the hydroxyl group attached to the left side of the
asymmetric carbon furthest from the carbonyl.
 D isomers have the hydroxyl group on the right side.
 Amino acid residues in naturally occurring protein molecules are
generally L-isomers
 D-amino acids are found only in a few peptides (eg. bacterial cell wall
and some antibiotics)

15. Classifying Standard Amino Acids
ESSENTIAL amino acids cannot be made by the body. As a
result, they must come from food.
 The 9 essential amino acids are: histidine, isoleucine, leucine,
lysine, methionine, phenylalanine, threonine, tryptophan, and
valine.

16. Classifying Standard Amino Acids
NON-ESSENTIAL amino acid perform a variety of functions in the
human body. Some non-essential amino acids like glutamine and
arginine, for example, can regulate gene expression and cell
signaling pathways, respectively. Other non-essential amino
acids help to control the digestion and absorption of nutrients.
 Nonessential amino acids include: alanine, arginine,
asparagine, aspartic acid, cysteine, glutamic acid, glutamine,
glycine, proline, serine, and tyrosine.

17. Based on Structure (functional
groups in the side chain)
• Alkyl/Aliphatic
• Sulfur-containing
• Alcohols
• Aromatics
• Acidic
• Basic
• Amides

18. Stabilize proteins through hydrophobic interaction
Alkyl/Aliphatic
Glycine
(Gly, G)
Alanine
(Ala, A)
Proline
(Pro, P)
Leucine
(Leu, L)
Isoleucine
(Ile, I)
Valine
(Val, V)

19. Cysteine is
responsible for
disulfide bridges in
proteins
Sulfur-containing
Cysteine
(Cys, C)
Methionine
(Met, M)
Methionine is very
hydrophobic

20. Stabilize protein and interact with the aqueous environment through hydrogen
bonding
Alcohols
Threonine
(Thr, T)
Serine
(Ser, S)

21. Aromatics
 Stabilize protein
through hydrophobic
interaction
 Aromatic amino
acids are
relatively nonpolar. T
o different degrees, all
aromatic amino acids
absorb ultraviolet light.
 Absorbance at 280
nm is used for
spectrophotometric
determination of
protein concentration
Phenylalanine
(Phe, F)
Tyrosine
(Tyr, Y) Tryptophan
(Trp, W)

22.  Have —COOH
side chains
which are
ionized at pH 7
 Negatively
charged
Acidic
Aspartic Acid/ Aspartate
(Asp, D)
Glutamic Acid/ Glutamate
(Glu, E)

23.  Have —NH2 side chains which are
protonated at pH 7; positively
charged.
 Lysine has a second primary group at
the epsilon position on its aliphatic
chain.
 Arginine has a positively charged
guanidinium group.
 Histidine has an imidazole group.
Histidine is the only common amino
acid having an ionizable side chain
with a pKa near neutrality.
 In many enzyme-catalyzed reactions,
a His residue facilitates the reaction
by serving as a proton
donor/acceptor.
Basic
Lysine
(Lys, K)
Arginine
(Arg, R)
Histidine
(His, H)

24. Amides
 Amide counterparts of
acidic amino acids
 Can stabilize protein by
hydrogen bonding
 The two amino acids
having R groups with a net
negative charge at pH 7
are aspartate and
glutamate each of which
has a second carboxyl
group
Asparagine
(Asn, N)
Glutamine
(Gln, Q)

25.  4-hydroxyproline – a
derivative of proline
 4-hydroxyproline can
be found in plant cell
wall proteins
 5-hydroxylysine –
derived from lysine
 Both are found in
collagen
Some Uncommon Amino Acids

26. Some Uncommon Amino Acids
• can be found in myosin
• found in prothrombin
(blood clotting protein

27. Some Uncommon Amino Acids
• found in elastin
• metabolites in the biosynthesis of
arginine and in the urea cycle

28. Helmenstine, Anne Marie, Ph.D. (2020, August
26). Protonation Definition and Example. Retrieved
from https://www.thoughtco.com/definition-of-
protonation-604621
PROTONIC EQUILIBRIA OF AMINO ACIDS
Protonation is the addition of a proton to
an atom, molecule, or ion. Protonation is
different from hydrogenation in that
during protonation a change in charge of
the protonated species occurs, while the
charge is unaffected during
hydrogenation. Protonation occurs in
many catalytic reactions.

29. Amino Acids are
Amphoteric
Amino acids are amphoteric compounds,
as they contain both acidic (COOH)
and basic (NH2) groups.

30. low pH high pH
Isoelectric point or pH (pI or IpH)

31. What are Peptide and
Peptide Bonds?
03

32.  A molecule that contains
two or more amino acids
(the molecules that join
together to form proteins).
 Peptides that contain many
amino acids are called
polypeptides or proteins.
 A peptide bond is formed by
a dehydration synthesis or
reaction at a molecular
level.
 This reaction is also known
as a condensation reaction
which usually occurs
between amino acids.
Peptide Peptide Bonds

33. As depicted in the figure, two
amino acids bond together to
form a peptide bond by the
dehydration synthesis. During
the reaction, one of the amino
acids gives a carboxyl group to
the reaction and loses a
hydroxyl group (hydrogen and
oxygen).
Formation of
Peptide Bonds

34. Biological Activities
of some Peptides
• As HORMONES (chemical
messengers of the body)
• INSULIN – responsible for the
absorption of glucose from the
blood stream
• OXYTOCIN – a non-apeptide that
stimulates uterine contraction

35. • VASOREPRESSIN – a
nonapeptide that prevents
urination at night
Biological Activities
of some Peptides
• Also known to regulate blood
pressure, blood osmolality,
and blood volume.

36. Synthetic Peptides
• ASPARTAME – a dipeptide
aspartylphenylalanyl methyl ester
used as artificial sweetener

37. is a short chain of amino acids.
Peptides

38. Drawing Peptides
Serine (N-terminal residue) → glycine → tyrosine → alanine
→ leucine (C-terminal residue) or SGYAL

39. Naming Peptides
•Start with the N-terminal residue
•Replace –ine of names with –yl for all
residues except that for the C-terminal
residue
•Write the whole name as one word
•serylglycyltyrosylalanylleucine

41. Sequence of Peptides
• Three-letter or single-letter designations
may be used
• Sequence: N-terminal to C-terminal residue

42. Properties of Peptide
Bond
•peptide bond (C—N) length: 0.133nm
•shorter than the adjacent C—N bond (0.145nm)
•longer than the C=O bond length of 0.123nm
0.123 nm
0.133 nm
0.145 nm

43. •Exhibits partial double bond character due to
resonance
•Semi-rigid bond
•Chemically stable – inert and not easily cleaved

44. No rotation around peptide bond

45. In contrast to the
peptide bond, the
bonds between the
amino group and
the α-carbon atom
and between the
α- carbon atom
and the carbonyl
group are pure
single bonds and
therefore can
rotate

46. Acid-Base Properties of Peptides
• All α-NH2 and α-COOH involved in peptide (amide) bond formation
are not anymore basic/acidic.
• Ionizable groups in a peptide include:
Amino group of the N-terminal residue
Carboxyl group of the C-terminal residue
side chains of the acidic and basic amino acids

47. — Tony Robbins
“The quality of your life is dependent upon the
quality of the life of your cells. If the
bloodstream is filled with waste products, the
resulting environment does not promote a
strong, vibrant, healthy cell life-nor a
biochemistry capable of creating a balanced
emotional life for an individual.”

48. Example:
Alanylglutamylglycyllysine

49. CREDITS: This presentation template
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Thank
you!
Please keep this slide for attribution
Presented by:
ALVERSADO, JHON MHER R.
NAMOCALE, KARIZA DONE
VILLAR, PIERRE ANGELIQUE

50. Amino Acid Structure - Definition, Structure, Basicity of Amino Acid with Examples. (n.d.). Retrieved from
https://byjus.com/chemistry/amino-acid-structure/
Zwitterion - Definition, Properties, Structure and Applications. (2022, August 18). Retrieved from
https://byjus.com/chemistry/zwitterion/
Enantiomers - Definition, Structure, Properties & Examples with Videos. (n.d.). Retrieved from
https://byjus.com/chemistry/enantiomers/
Gevorg, D. S. (2020, December 1). D and L Sugars - Chemistry Steps. Retrieved from https://www.chemistrysteps.com/d-
and-l-sugars/
Peptide Bond - Definition, Formation, Structure, Examples. (n.d.). Retrieved from https://byjus.com/jee/peptide-bond/
NCI Dictionary of Cancer Terms. (n.d.). Retrieved from https://www.cancer.gov/publications/dictionaries/cancer-terms
P. (n.d.). Glycine. Retrieved from https://pubchem.ncbi.nlm.nih.gov/compound/750
P. (n.d.). Cysteine. Retrieved from https://pubchem.ncbi.nlm.nih.gov/compound/5862
References