Proteins are made up of amino acids and have various structures and functions in the body. They provide energy, structure and are involved in processes like metabolism, immune function and cell repair. There are over 100,000 different proteins in the human body, each with distinct roles. Proteins have primary, secondary, tertiary and quaternary levels of structure which determine their shape and function. It is important to consume a variety of protein sources to meet nutritional needs. Both deficiencies and excesses of protein can impact health.

1. PROTEINS
Tina-Joven-Buenafe

2. Introduction
 Greek word ("prota")
 meaning "of primary importance"
 Jöns Jakob Berzelius

3. Proteins
 Atoms: C, H, O, N, P, S
 Basic units: amino acids (20)
 Provide energy & structure, repairs body
tissues
 Some are called hormones, enzymes,
neurotransmitters, etc.
 Foods high in protein: meat, eggs, poultry,
milk & milk products, nuts, dried beans,
peas, & lentils

4. Protein Facts
 Proteins are big molecules called
macromolecules
 Made of smaller molecules called amino
acids
 Made of carbon, hydrogen, oxygen, nitrogen,
sulfur, & some other elements
 There are at least 100,000 proteins in your
body
 Each has a different structure that gives it a
specific job.
 There are 4 types of structure, including coils
& curls.

6. Amino Acids
 Think of proteins as being like a
word. Amino acids are the letters
in that word. Rearranging the
letters makes words with
different meanings.
 There are 20 amino acids
required for human life to exist.
 12 amino acids are made in our
bodies, but the other 8 must be
obtained by eating foods that
contain them.

7. Enzymes
 Some proteins curl up into a shape
like a ball of enzymes.
 An enzyme is a special protein & a
catalyst for a chemical reaction in
living things.
 Catalysts speed up the rate of a
reaction.
 Enzymes are needed for many
chemical reactions in your body.
 Without them, these reactions would
occur too slowly to keep you alive.

8. Proteins in the Diet
 It ’ s important to have lots of
protein in your diet!
 Proteins in foods such as meats,
soybeans, & nuts are broken
into amino acids.
 Without protein, your body can’t
function perfectly..
 This is why it ’ s important for
vegetarians to find protein from
non-animal sources.

9. Proteins
*The most common organic compound that contains
nitrogen as well as carbon, hydrogen and oxygen.
*Some proteins also contain sulfur and phosphorus.
*For support, structure, movement, transport,
communication and disease defense.
Protein containing structures in vertebrate animals include
hair, nails, hooves, cartilage, hormones, muscles, many
poison,and enzymes.
*Enzymes- are catalysts that speed up chemical
reactions

10. Proteins
Amino acids-the building blocks of protein are the
primary structural units of protein, composed of
amino group (-NH 2 ) on one end and a carbonyl
group (-COOH).
Essential amino acids-the known standard amino acids
ex. alanine, arginine, asparagine, aspartic
acid, cysteine, glutamic acid, glutamine, glycine, histidine,
isoleucine, leucine, lysine, methionine, phenylalanine,
proline, serine, threonine, tryptophan, tyrosine, and valine.

11. Proteins
* Essential amino acids are found in adequate amounts in
protein-rich foods from animals or in combinations of plant
proteins
***there are 150 other amino acids which can be found in
nature, mostly in fungi and higher plants.
***amino acids have similar chemical structure but differ
in a region called R group
*** R group are ionically charged, some are polar, and
some are non-polar. Thus, the R group gives each amino
acid its own characteristics.

12. Proteins
Proteins have four types accdg’ to bonding
1. Primary- sequence of amino acid in protein
2. Secondary- based on hydrogen bonds between amino
acids, causing helical structure of a protein
3. Tertiary- the folding and bending of the polypeptide
chain
4.Quarternary –composed of number of polypeptide chains
covalently bonded together such as hemoglobin and
insulin

13. Proteins
Primary Structure
 The very basic strand
of amino acids
Secondary Structure
 The hydrogen-bond
interaction among strands of
amino acids giving alpha
helices and beta-sheets
shapes .

14. Proteins
Tertiary Structure
 Interaction between
alpha helices and beta-
sheets.
 These protein domains
for small globular
proteins.
Quaternary Structure
 Small globular proteins
form protein
aggregates.
 A famous example is
hemoglobin.

15. Protein Structures

16. Protein Structures (Cont’d)

17. Enzymes
Are proteins
Speed up chemical reactions without
being consumed or using energy
Enzymes
 Amylase - breaks down sugar
 Proteases - break down proteins
 Lipases - break down lipids
 Catalase - breaks down hydrogen
peroxide

18. urease
introduction
(NH2)2CO + H2O → CO2 + 2NH3
James B. Sumner

19. hemoglobin
introduction
Max Perutz

20. myoglobin
introduction
Sir John Cowdery Kendrew

21. Protein in the Human Diet
 important macronutrient in the human diet,
supplying the body's needs for amino acids
 Methionine Leucine
 Threonine Phenylalanine
 Lysine Tryptophan
 Valine (Histidine)
 Isoleucine (Arginine) - spermatogenesis

22. proteins in the human diet

23. proteins in the human diet

24. proteins in the human diet

25. proteins in the human diet

26. proteins in the human diet

27. Major Functions of Proteins
1. Enzyme catalysis (saliva)
2. Transport and storage (hemoglobin)
3. Immune protection (dendrotoxins)
4. Signaling (Rhodopsin)
5. Structural support (collagen, keratin)
6. Coordinated motion (myosin, kinesin)
7. Control of growth and differentiation

28. Classifications of Proteins
I. Simple Proteins
 True proteins
 Yield a-amino acids and their derivatives

29. Solubility Heat Coagulation Examples
a. Albumins Soluble in water and dilute
neutral salt
Coagulated by heat Serum albumin
Ovalbumin
lactalbumin
b. Globulins Soluble in neutral salt solution
Insoluble in water
Coagulated by heat Ovoglobulin
edestin
legumin
myosinogen
serum globulin
c. Glutelins Soluble in dilute acids and
alkalies
Insoluble in neutral solvents
Glutenin
oryzenin
d. Prolamines Insoluble in ordinary solvents
Soluble in 70% alcohol
Not coagulated by heat Gliadin
Zein
hordein
e. Histones Soluble in water, dilute acids
and alkalies
Insoluble in dilute ammonia
Not readily coagulated
by heat
Globin
thymus histone
scobrone
f. Protamines Soluble in water and dilute
acids and alkalies
Not coagulated by heat Salmin
g. Scleroproteins
(albuminoids)
Insoluble in water and neutral
solvents
Keratin
Elastin
collagen

30. classifications of proteins
II. Conjugated Proteins
 Made up of protein molecules combined
with non-protein groups

31. Properties Examples
a. nucleoproteins Combination of histones and
protamines with nucleic acid
Soluble in dilute solutions of NaCl
and can be extracted from the
tissues by the use of this solvent
Chromatin
Glandular tissues
Germ of grains
b. glycoproteins Proteins with a carbohydrate
component
Lubricating purposes
Mucin
Tendomucoid
Ossemucoid
c. phosphoproteins Prosthetic group (H3PO4) joined to
the protein molecule
Casein
Vitelin
4. chromoproteins With hematin or similar pigments Hemoglobin
Cytochromes
Rhodopsin
5. lipoproteins Fatty substances combined with
their molecules like lecithin and
cephalin
Blood serum, Brain tissues,
Cell nuclei, Egg yolk, milk

32. classifications of proteins
III. Derived Proteins
 Substances formed from simple and
conjugated proteins
A. Primary protein derivatives
B. Secondary protein derivatives

33. Primary protein Properties Examples
a. proteans Insoluble substances resulting from
the preliminary action of water,
dilute acids or enzymes
Myosan
Edestan
b. metaproteans Products of further hydrolysis
Soluble in weak acids and alkalies
Insoluble in neutral salt solutions
Acid
metaproteans
Alkali
metaproteans
c. coagulated
proteins
Insoluble products resulting from
either the action of heat, alcohol,
ultraviolet rays or even simple
mechanical shaking
Cooked egg
albumin
Cooked meat

34. Secondary
protein
Properties
a. primary
proteoses
Soluble in water
Precipitated by HNO3
Not coagulated by heat
b. secondary
proteoses
Precipitated only by complete saturation with ammonium
sulfate but not with nitric acid or picric acid
c. peptones Soluble in water
Not coagulated by heat
Not precipitated by saturation with ammonium sulfate
Precipitated by alkaloidal reagents, such as,
phosphotungstic and tannic acids
d. peptides Combinations of two or more amino acids, the carboxyl
group of one being united with the amino group of the
other
Properties like peptones
Di, tri, tetra, penta, and polypeptides

35. Amino Acids
 Building blocks of proteins
 Contain:
 Amine
 Carboxyl functional groups
 H2NCHRCOOH

36. General Structure

37. Classification
1. Neutral amino acids
a. Aliphatic amino acids
b. Aromatic amino acids
c. Thionine group
d. Secondary amino acids
2. Acid amino acids
3. Basic amino acids

39. Aliphatic amino acids
 Glucogenic
 Create muscle tissue
 Healthy CNS and DS
 Regulate blood sugar
 Potential cancer
treatment

40. Aliphatic amino acids
 Eliminate excess toxins
 Protect cells
 Balanced levels of
nitrogen and glucose
 Maintain glucose levels

41. Aliphatic amino acids
 Derived from glycine
 Brain and CNS
 Forms phospholipids
 Fat, fatty acid
metabolism; muscle
formation; immune
system

42. Aliphatic amino acids
 Normal growth
 Repair tissues
 Blood sugar level
 Stimulate CNS
 Remove toxic excess
nitrogen
 Treat liver and
gallbladder diseases

43. Aliphatic amino acids
 Normal growth
 Protein balance
 Cardiovascular, liver,
CNS, and immune system
 Connective tissues,
muscles, bones, tooth
enamel
 Treats depression

44. Aliphatic amino acids
 Repair muscles
 Regulate blood sugar
 Provide energy
 Growth hormones
 Burn visceral fat
 Promote healing of bones,
skin and muscles
 Recovery from surgery

45. Aromatic amino acids
 Functioning of CNS
 Controls depression
and chronic pain
 Treating brain disorders
 Aggravate high blood
pressure or migraines

46. Aromatic amino acids
 Regulate mood
 Stimulate CNS
 Thyroid, pituitary,
adrenal glands
 Treatment: allergies,
headaches, Parkinson’s
disease, drug
withdrawal

47. Aromatic amino acids
 Sleeping aid
 Antidepressant
 May treat Parkinson’s

48. Thionine group
 Form healthy skin, hair,
bones and connective tissues
 Remove toxins (alcohol,
cigarette)
 Prevent hangovers
 Anti-aging
 Treat emphysema, TB, and
bronchitis

49. Thionine group
 Process and eliminate fat
 Form healthy collagen
 Help treat Pancreatitis
and Parkinson’s; UTI;
arthritis; depression

50. Secondary amino acids
 Produce collagen and
cartilage
 Keep muscles and joints
flexible
 Reduce sagging and
wrinkling
 Treat osteoarthritis,
chronic back pain

51. Acid amino acids
 Important in TCA cycle
 Treat chronic fatigue
 Increases stamina and
endurance levels
 Produce immune
system proteins
 Removes excess NH3

52. Acid amino acids
 Excitatory neurotransmitter
 Build muscle (supplement)
 Reduce body fat
 Reduce cirrhosis

53. Basic amino acids
 Antiviral properties
 Prevent herpes and cold
sores
 Growth of bones

54. Basic Amino Acid
 Keep liver, skin, joins
and muscles healthy
 Regulates hormones
 Promotes male fertility
 Treat impotence and
heart disease
Arginine (Arg/R)

55. Basic amino acids
 Maintain healthy tissues
 Treat mental disorders
and sexual dysfunction
 Relieve rheumatoid
arthritis
 Natural detoxifier

56. Protein Structure
 arranged in a linear chain and joined
together by peptide bonds between
the carboxyl and amino groups of
adjacent amino acid residues.

58. Structure of Proteins
1. Primary structure
2. Secondary structure
3. Tertiary structure
4. Quaternary structure

60. Protein Deficiency and
Dietary Imbalance
 fatigue
 insulin resistance
 hair loss
 loss of hair pigment
 loss of muscle mass
 low body temperature
 hormonal irregularities
 loss of skin elasticity
 Kwashiorkor

61. Excessive Protein Intake
 Liver dysfunction
 Loss of bone density