CHEMICALOFREACTIONS
PROTEINS
Hyof dpr ort eoi nlsybys: is
acids
bases
enzymes
organic acids are
more effective than
the mineral acids in
liberating the
ammonia, NH3 from
its amides.
cause very rapid
and complete
hydrolysis like the
deamination of
certain amino
acids.
pepsin
hydrolyzes
proteins to
proteoses,
peptones and
polypeptides
only.
iotpe i nits ation
c
e
r
P of pr by:
proteins react with acids because of
their free amino groups.
The acids are termed as alkaloidal
reagents because they precipitate
many of the alkaloids.
acids
PROTEIN
DENATURATION
is the change in the chemical, physical and biological properties of a
protein and characterized by an unfolding of the molecule. It destroys the
physiological function of the protein
PROTEINS
comes from the Greek πρώτα ("prota"), meaning
"of primary importance".
50% Carbon (C), 7% Hydrogen (H) , 23%Oxygen
(O) , 16% Nitrogen (N), and some contain 0 3%Sulfur (S) and 0-3% Phosphorus (P)
are essential parts of organisms and participate in
every process within cells.
SOURCES
Plants synthesize proteins from inorganic
substances present in air and soil.
Animals obtain proteins when they eat plants or
other animals. Animals excrete waste materials
containing many nitrogen compounds which, along
with decaying and plant matter, are converted into
soluble nitrogen substances. Plants in turn use this
soluble nitrogen to manufacture more protein.
Denaturing Agents
PHYSICAL AGENTS
heat - disrupts all types of bonds
other agents: light, surface action, high pressure, mechanical agitation
CHEMICAL AGENTS
1.) alcohol - forms hydrogen bonds that compete with the naturally occurring
hydrogen bonds
2.) salts of heavy metals - disrupts salt bridges and the disulfide bonds
present in the protein
3.) alkaloidal reagents - disrupts salt bridges and hydrogen bonds
4.) radiation - disrupts hydrogen bonds and hydrophobic interactions
5.) changes in pH - disrupts hydrogen bonds and salt bridges
6.) oxidizing and reducing agents - disrupts disulfide bonds
7.) salting out - most proteins are insoluble in saturated salt solutions and
precipitate out unchanged
citations:
I. information
CHAPTER 4: PROTEINS. (n.d.). In Chem 2 Biochemistry (pp. 54–70). Retrieved from
PDF.
Sanvictores, T. (2022b, October 31). Biochemistry, primary protein structure.
StatPearls - NCBI Bookshelf. https://www.ncbi.nlm.nih.gov/books/NBK564343
Admin. (2023, July 14). Amino acids- properties, functions, sources and its
deficiency disorders. BYJUS. https://byjus.com/biology/amino-acids/
II. illustrations
CHAPTER 4: PROTEINS. (n.d.). In Chem 2 Biochemistry (pp. 55-68). Retrieved
from PDF.
Ashjaee, N. (2019). Types of Protein Structures. Learn About the 4 Types of
Protein Structure. Retrieved from https://www.thoughtco.com/proteinstructure-373563.
PROTEINS
PROTEINS
PROTEINS
PROTEINS
PROTEINS
PROTEINS
PROTEINS
Submitted by: Damielle Mae B. Ofqueria
Program and Section: BSN 1-H
Schedule: 7:30-12:00 NN, Monday and Wednesday
SAPSESCIFIIFCIACTI
FUNCTIONS
FUNCTIONS
O ACID
N
I
M
A
S
STR
UCTURE
P
interaction
with water
examples:
Egg albumin; serum albumin;
lactalbumin
Serum globulin;
lactoglobulin; vegetable
globulin
Keratin in hair, nails,
feathers; collagen
Nucleohistone in thymus
gland; globin in hemoglobin
protein type
solubility
albumins
soluble in water & salt solutions
globulins
slightly soluble in water;
soluble in salt solutions
albuminoids
insoluble in all neutral solvents
and in dilute acid & alkali
histones
soluble in salt solutions;
insoluble in very dilute NH4OH
prosthetic group
composition
Nucleoproteins
Nucleic acid
CONJUGATED PROTEINS TO THE NATURE IF THEIR
PROSTHETIC GROUP
Glycoproteins
Carbohydrates
Phosphoproteins
Chromoproteins
Chromophore group
Lipoproteins
Lipids
Metalloproteins
Metals
storage
structural
hormones
Collagen, Keratin
toxins
Ferritin
transport
Hemoglobin, Serum
albumin
protective
contractile
enzymes
Myosin, actin
Pepsin
Venoms
Gamma globulin,
Fibrinogen
exist as long stranded molecules
for structural support
globular proteins
have somewhat spherical shapes.
myoglobin
structure
collagen structure
ju g ate
derived
LEVELS OF PROTEIN
STRUCTURES
Primary Structure
the sequence of amino acids linked
together to form a polypeptide chain.
It refers on the regularly repeating local
structures stabilized by hydrogen bonds.
The most common examples are the alpha
helix and beta sheet.
Tertiary Structure
Refers to the specific folding and
bending of the coils into specific
layers and gives proteins their specific
biologic activity.
Quaternary Structure
gross structure
PROPERTIES
on
Secondary Structure
Phosphate
function
soluble in water
(insoluble in
organic solvents)
si m ple
type
Insulin
white crystalline
solid
PROTEINS
d
solubility
fibrous proteins
high melting and
boiling point
OF
according to:
SIMPLE PROTEINS CAN BE
CLASSIFIED T0:
SIFICATIONS
S
A
CL according to
-Group
CLASSIFICATION
CL ROOTFEINS ON
c
Are biological catalysts (enzymes)
Are antibodies that fight antigens (bacteria and viruses)
Transport molecules and ions (hemoglobin)
Regulate cell function
Provide structural support and mechanical strength
(skin)
Are necessary for all forms of movement / muscular
activity
Are sources of amino acids for growth
Regulate metabolic processes (hormones)
Transmission of impulses (nerves)
Transmission of hereditary characteristics
(nucleoprotein)
GENERAL
The shape or structure that results from the
interaction of more than one protein molecule
(protein subunits) which function as part of the
larger assembly or protein complex.
This occurs when two or more protein units, each
with own primary, secondary & tertiary structure;
combine to form a more complex unit.