Proteins are the most abundant and functionally diverse molecules in living systems, composed of amino acids linked by peptide bonds. They can be classified in various ways, including by molecular structure (globular vs fibrous), solubility, presence of non-protein groups, function (enzymes, hormones, etc.), and nutritional quality. The 20 primary amino acids are the building blocks of all proteins in plants and animals, and each has a specific genetic codon in mRNA.
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...Tiffy John
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, PRIMARY, SECONDARY, TERTIARY AND QUATERNARY STRUCTURE, FIBROUS AND GLOBULAR STRUCTURE, SOURCES, TYPES OF PROTEINS, FUNCTIONS,DEFICIENCIES
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, ...Tiffy John
Proteins , INTRODUCTION, GOOD PROTEINS, BAD PROTEINS, STRUCTURE OF PROTEINS, PRIMARY, SECONDARY, TERTIARY AND QUATERNARY STRUCTURE, FIBROUS AND GLOBULAR STRUCTURE, SOURCES, TYPES OF PROTEINS, FUNCTIONS,DEFICIENCIES
This is a continuation of the earlier slide with a name "Nucleotides". Please refer to the previous mentioned slide before moving to this slide for a better overall concept on nucleotides and nucleic acids.
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
This is a continuation of the earlier slide with a name "Nucleotides". Please refer to the previous mentioned slide before moving to this slide for a better overall concept on nucleotides and nucleic acids.
Amino acids are biologically important organic compounds composed of amine (-NH2) and carboxylic acid (-COOH) functional groups, along with a side-chain specific to each amino acid. The key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen, though other elements are found in the side-chains of certain amino acids. About 500 amino acids are known and can be classified in many ways. They can be classified according to the core structural functional groups' locations as alpha- (α-), beta- (β-), gamma- (γ-) or delta- (δ-) amino acids; other categories relate to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic, containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids comprise the second-largest component (water is the largest) of human muscles, cells and other tissues.Outside proteins, amino acids perform critical roles in processes such as neurotransmitter transport and biosynthesis.
Proteins are the macromolecules responsible for the biological processes in the cell. They consist at their most basic level of a chain of amino acids, determined by the sequence of nucleotides in a gene. Depending on the amino acid sequence (different amino acids have different biochemical properties) and interactions with their environment, proteins fold into a three-dimensional structure, which allows them to interact with other proteins and molecules and perform their function
essential topic on bio molecule:
They are naturally occurring polypeptides that contain more than 50 amino acid units. therefore a protein is a hetero polymer.
Most abundant organic molecules of the living system.
They form about 50% of the dry weight of the cell.
They are most important for the architecture and functioning
of the cell.
Proteins on complete hydrolysis yields Amino Acids
There are 20 standard amino acids which are repeatedly found in the structure of proteins – animal, plant or microbial.
Collagen is the most abundant animal protein and Rubisco is the most abundant plant protein
Protein Synthesis is controlled by DNA.
They are substituted methane (CH4)
Amino acids are group of organic compounds having 2 functional groups (-NH2) and (-COOH)
(-NH2) group is basic whereas (-COOH) is acidic
R- can be H in glycine, CH3 in alanine, Hydroxymethyl in serine
in others it can be hydrocarbon chain or a cyclic group
All amino acids contain C, H, O and N but some of them additionally contain S
Physical and chemical properties of amino acids are due to amino, carboxyl and R functional groups
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.
based on class feedback, i've switched the presentations to a black&white template. this is easier to see in classroom presentation and most.definitely easier to print out legible notes!
Biomolecules Proteins and Amino Acids.pptxSejalWasule
Biomolecules are molecules that are essential for life. They are organic compounds that are synthesized by living organisms and are involved in many of the processes that sustain life. There are four main categories of biomolecules: carbohydrates, lipids, proteins, and nucleic acids. Proteins are biomolecules that are composed of long chains of amino acids. They are involved in a wide range of cellular functions, including catalyzing chemical reactions, providing structural support, and transporting molecules across cell membranes. Proteins can also act as enzymes, which are molecules that catalyze specific chemical reactions in the body.
Nucleic acids are biomolecules that are composed of nucleotides. There are two main types of nucleic acids: deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). DNA contains the genetic information that is passed from one generation to the next, while RNA is involved in protein synthesis. Overall, biomolecules are essential for the functioning of living organisms and are involved in many of the processes that sustain life. Proteins are large, complex molecules that are essential to life. They are composed of long chains of amino acids, which are organic compounds that contain both an amino group (-NH2) and a carboxyl group (-COOH) bound to the same carbon atom. The sequence of amino acids in a protein determines its structure and function.
There are 20 different types of amino acids that can be incorporated into proteins. Each amino acid has a unique side chain, which determines its chemical properties. Some amino acids are hydrophobic (repel water), while others are hydrophilic (attract water). Amino acids can also be acidic or basic, and some have other unique properties, such as the ability to form disulfide bonds.
When amino acids are joined together by peptide bonds, they form a polypeptide chain. The sequence of amino acids in the chain determines the shape of the protein, which is critical to its function. Proteins can have several levels of structure, including primary, secondary, tertiary, and quaternary structure. Primary structure refers to the linear sequence of amino acids in the polypeptide chain. Secondary structure refers to the regular patterns of folding that occur within the polypeptide chain, such as alpha helices and beta sheets. Tertiary structure refers to the overall three-dimensional shape of the protein, which is determined by the interactions between the amino acid side chains. Quaternary structure refers to the way that multiple polypeptide chains come together to form a functional protein. Proteins have many important roles in the body, including catalyzing chemical reactions (as enzymes), transporting molecules across cell membranes (as transport proteins), and providing structural support (as collagen). They are also involved in the immune system (as antibodies), signaling pathways (as receptors), and energy metabolism (as enzymes and carriers).
2. Proteins are the most abundant and functionally
diverse molecules in living systems where they
constitute 50% or more of their dry mass.
The word protein is derived from the Greek Protos,
which means the first or supreme.
Proteins are nitrogenous macromolecules,composed
of aminoacids linked by peptide bond.
3.
4. AMINO ACIDS
Amino acids are organic solvents.
Have two functional groups –NH₂ and
-COOH group.
The amino group is basic while carboxylic group is
acidic in nature.
Soluble in water but insoluble in organic solvents
e.g chloroform,acetone,ether,etc.
All amino acids which make up proteins are L-α-
aminoacids.
All amino acids have chiral carbon, exept Glycine.
5.
6.
7.
8.
9. LOW pH NEUTRAL HIGH pH
O O O
R C R C R C
OH O O
NH3 NH3 NH2
ammonium Form Zwitterion Carboxylate Form
10. CLASSIFICATION OF AMINO ACIDS
Although more than 300 naturally
occurring amino acids are known but only
20 amino acids take part in the formation
of all types of proteins,plants as well as
animal in origin.
These 20 amino acids are known as
Primary,Standard or normal amino acids.
11. Each of these amino acids has one or
more genetic codon(s) which are present
within the molecules of specific mRNA
which themselves are produced under
direction of genes occuring in DNA
molecules.
12.
13.
14.
15.
16.
17.
18.
19.
20.
21.
22. Semi-essential aminoacids.
These include Arginine and
Histidine.These are growth promoting
factors since they are not synthesized in
sufficient quantity during growth.
28. Non protein amino acids
These are the amino acids which donot
take part in the protein synthesis, and have
no genetic codes.They perform other
functions in human metabolism e.g
37. Proteins are made by controlled polymerization of amino acids
water is eliminated
O O
two amino acids H2N CH C OH H2N CH C OH
condense to form...
R1 R2
N or amino C or carboxy
terminus O O terminus
...a dipeptide. If H2N CH C NH CH C OH + HOH
there are more it
becomes a polypeptide. R1 R2
Short polypeptide chains
are usually called peptides
while longer ones are called peptide bond is formed
proteins.
residue 1 residue 2
38. Classification of peptides
DIPEPTIDES
OLIGOPEPTIDES
Composed of 3-10 amino acids linked
together through peptide bond.e.g
Tripeptide(3 amino acids linked together
by 2 peptide bonds),Tetrapeptide(4 amino
acids linked together by 3 peptide bonds).
47. UNUSUAL PEPTIDE BOND
In some cases the peptide bond in a
peptide does not involve α-COOH
group.e.g Glutathione which has the
sequence glutamic acid,cysteine and
glycine.However,the –COOH group of
glutamic acid forming peptide bond with
cysteine is not α but γ.For this reason
glutathione is chemically γ-glutamyl-
cysteinyl-glycine.
48. CLASSIFICATION OF
PROTEINS
ON THE BASIS OF MOLECULAR LENGTH
AND SHAPE.
Fibrous proteins.
When the axial ratio of length:width is more
than 10.e.g collagen,α keratin of hair.
Globular proteins.
When axial ratio of length:width of protein
molecule is less than 10.e.g
Myoglobin,haemoglobin,ribonucleases.
49. ON THE BASIS OF SOLUBILITY AND
PHYSICAL PROPERTIES.
Simple proteins
Conjugated proteins
Derived proteins
50. SIMPLE PROTEINS
These are the proteins which on complete hydrolysis yield
only amino acids.They are further classified based on
their solubilities and heat coagulabilities.
1.ALBUMIN
Soluble in water
Precipitated by full saturation with ammonium sulfate
Coagulated by heat
Examples,Ovalbumin.serum albumin,lactalbumin and
legumel
51. 2.Globulins
Insoluble in water,soluble in dilute salt
solutions.
Heat coagulable
Precipitated by half saturation with
ammonium sulfate.
Examples,serum
globulins,lactoglobulin,myosin in
muscles,ovoglobulin and legumin.
52. 3.Globins
Rich in histidine but not basic.
Combine with heme to form hemoglobin.
4.Prolamins
Soluble in ethanol,insoluble in water.
Rich in amino acid proline but deficient in
lysine.
Examples,gliadin of wheat and zein of maize.
53. 5.Protamines.
Basic proteins,soluble in NH4OH.
Rich in arginine,lack tyrosine and
tryptophan.
Form nucleoproteins with nucleic acids.
Present in sperm cells.
56. COPOUND OR CONGUGATED PROTEINS
These are the proteins which in addition to
amino acids contain contain a non protein
group called prosthetic group in their
structure.
1.Nucleoproteins
Histones+nucleic acids
Most abundant in tissues having a large
proportion of nuclear material e.g
yeast,thymus and other glands and sperms.
57. 2.Phosphoproteins
Simple proteins+phosphoric acid
Examples casein of milk and vitellin of egg yolk.
3.Lipoproteins
Simple proteins+covalently bonded with lipid
substances like lecithin,cholesterol,triglycerides
and fatty acids.
Occur in blood plasma,nervous tissue,egg
yolk,milk and cell membrane.Bacterial antigens
and viruses also contain lipoproteins.
60. DERIVED PROTEINS
Include proteins derived from simple and
conjugated proteins.
1.Primary derived proteins
Synonymus with denatured proteins.
Denaturation takes place when some or all of
the cross linkages which normally keep the
molecular of protein intact are split,although
there is no hydrolysis of protein molecule.
61. Denaturation may be brought about by
chemical or physical agents such as heat,X
rays,ultrasonic waves,shaking or stirring for
long time,extremes of pH,salts of heavy
metals,neutral chemical agents such as urea
and organic solvents such as alcohol and
acetone.
In most cases denaturation is irreversible,but
in some cases it is reversible
Example,RIBONUCLEASE.(Denaturation is
reversible)
62. Secondary derived proteins
These substances are intermediates formed in the
progresive hydrolysis of protein molecule.They are of
different sizes and different amino acid composition.
PROTEOSES
Soluble in water,coagulated by heat,and are precipitated
from their solution by saturation with ammonium
sulphate.
PEPTONES
POLYPEPTIDES
OLIGOPEPTIDES
63. Classification based on function.
Catalytic proteins
Regulatory or hormonal proteins
Transport prpoteins
Immune proteins
Contractile proteins
Genetic proteins
Peptide bond formation is not spontaneous (favorable in free energy) under normal conditions, and requires conversion of the carboxyl or the amino group to a form which reacts more readily. In general, the carboxylic acid moiety is activated by converting it to an ester, acid chloride, anhydride, azide or some other derivative that makes the carbonyl group more nucleophilic. Note that once you make a peptide bond, the peptide backbone is fairly chemically inert: the nitrogen is no longer as strong a nucleophile, and the linkage is pretty stable and slow to hydrolyze. Proteins are typically digested exhaustively by heating to near boiling temperatures in reasonably strong solutions of hydrochloric acid. As we will learn later, there are of course enzymes that hydrolyze proteins quite efficiently.