BIOMOLECULES
SRIRAMAKRISHNAN.E
I M.Sc. Biotechnology
Department of Biotechnology and Microbiology
National College (Autonomous), Trichy, Tamil Nadu, India
The major classes of biological molecules
that are important for all living organisms are
• carbohydrates
• Lipids
• proteins
• Nucleic acids
CARBOHYDRATES
• Carbohydrates - compounds that are made of C, H, and O
• Examples: all sugars, starches, cellulose and chitin are Carbohydrates
used for energy storage and structures.
• Carbohydrates have a caloric value of 4.1 kilocalories/gram.
• The simplest class of carbohydrates are monosaccharides - simple sugars- All have
3 to 6 carbons
• 6 carbon sugars
Simple sugars
exist in different
forms and can be
drawn in different
ways
• The six carbon sugars all
have the same chemical
formula: C6H12O6
• They differ in the
placement of functional
groups C=O and -OH
• Isomers have the same
chemical formula .
• Stereoisomers differ in the
arrangement of a functional
group at a single carbon
• Monosaccharides are the
building blocks of more
complex carbohydrates
• For example. Sucrose and
lactose are a combination
of two monosaccharides
• Disaccharides
are formed by
GLYCOSIDIC
linkage by the
removal of
water molecule
• Polysaccharides are polymers of
monosaccharides.
• Polymers are long chain
molecules with repeating
subunits
• Starches are polymers of glucose
• Each glucose molecule is an
energy rich molecule
• Amylose is an unbranched chain
and is produced by plants.
Amylopectin is branched and
also produced by plants.
• Glycogen is highly branched and
produced by animals
• Starch is a polymer of α- glucose
and it is readily soluble
• Cellulose is a β-glucose and
indigestible
• Cellulose is a structural
polysaccharide and used for
construction of cell wall synthesis
by plants.
• Another important
polysaccharide is chitin which is
made up of β-glucose molecule
that have nitrogen containing
functional group.
• chitin is used for the
construction of cell wall in fungi.
LIPIDS
• Lipids - a chemically diverse class of organic molecules that are
grouped together because they are all largely nonpolar.
• Because they are nonpolar in nature they are soluble in organic
solvents like chloroform, benzene, acetone, paint thinner, etc.
and insoluble in water
• The major classes of lipids are fatty acids, neutral fats,
phospholipids, steroids
• Lipids have many functions including energy storage, cell
membrane structure, vitamins and hormones
Saturated fatty acid
Unsaturated fatty acid
• Fatty acids are long-chain
carbon molecules with many
carbon- hydrogen bonds and a
carboxyl group (COOH) on one
end.
• The carboxyl group can ionize,
releasing an H+
• Saturated fatty acids have no
C=C bonds - all carbons in the
chain are bonded to as many
hydrogens as possible
• Unsaturated fatty acids have
some C=C bonds in the chain -
the carbon chain is not
completely saturated with
hydrogens.
• Phospholipids - structural lipids - an integral part of cell
membranes - inside and enclosing cells.
• Structurally similar to triglycerides - one fatty acid is replaced by a
choline group.
• The choline group has both N and P in its structure
• The choline group is charged (polar) and will hydrogen bond with
water. It is called hydrophilic .
• The rest of the molecule is nonpolar and insoluble in water. It will not
hydrogen bond with water. It is hydrophobic.
• The choline end of the
molecule is called the
“head.”
• The fatty acid chains are
called the “tails.”
• Phospholipids have
hydrophilic heads and
hydrophobic tails
• In water, phospholipids
spontaneously form
micelles or bilayers
BIOMOLECULES.pdf
• Steroids or Sterols
- have a more complex
structure than other lipids
and a greater diversity of
functions
• Cholesterol is an important
part of cell membranes
• Vitamin D is necessary for
some biochemical reactions
to occur properly
Vitamin D
PROTEINS • Proteins – the most functionally diverse class
of biological molecules - Protein diversity is
the basis of the diversity of life.
• Everything that organisms are composed of -
all parts - are made of, or by proteins
• Proteins serve as enzymes, for defense,
transport, support, motion, regulation, and
storage
• There are 20 different amino acids used in
proteins. All have a similar structure.
• All have a central carbon, an amino group
(NH2) and a carboxyl group (COOH).
• Proteins are polymers of amino
acids joined through peptide
bonds.
• The carboxyl group (COOH) of
one amino acid links with the
amino group (NH2) of another to
produce the sequence CONH and
release water forms a peptide
bond (H2O)
BIOMOLECULES.pdf
• The diversity of protein function results from diversity ofprotein structure which
is the result of variation in the sequence of amino acids
• Functional proteins can vary in length from about 50 aminoacids to several
thousand amino acids
• The variety of amino acid sequences that are possible for proteins is practically
infinite.
• The diversity of amino acid sequence results in diversity of protein structure
Protein structure can be classified at several different levels: primary, secondary,
tertiary, and quaternary.
• Primary structure - the
amino acid sequence by the
polypeptide bonds
• Met - Gly - His - Trp - Lys - ...
• Secondary structure - the
regular coiling and bending of
the polypeptide that results
from hydrogen bonding of
amino and carboxyl groups in
different amino acids.
• This forms have 2
characteristic structures - the
a helix and the b-pleated sheet
• R groups of different amino acids
can interact in a variety of ways
to produce more complex
structure
• Hydrogen bonds are weak
interactions between polar R
groups
• Some R groups form covalent
bonds or ionic bonds
• Nonpolar R groups can have a
weak attractive interaction
• Because nonpolar R groups are
hydrophobic they are found in the
interior of proteins
• Tertiary structure - the bending
and folding of the polypeptide in
3-D space due to the interactions
of the R groups distant amino
acids
• Interactions include: bonding,
ionic bonding, covalent bonds,
hydrophobic interactions,
hydrophilic interactions
• Quaternary structure - the
interaction of different
polypeptides
• Quaternary structure is the result
of the same interactionsas above.
• Not all proteins have quaternary
structure
• Protein structural diversity is responsible for the functional diversity of proteins.
• Protein shape causes protein function
• Small changes in shape can influence function
• Proteins are sensitive to environmental changes.
• Change in pH, temperature, ion concentration can all
cause a change in the shape of the protein and influence its functional properties
• High temperatures result in weakening of H-bonds.
• Proteins tend to denatures (unfold) at high temperature.
• Low temperatures strengthen H-bonds.
• Proteins become rigid at low temperature.
NUCLEIC ACID
• Nucleic acids - nucleic acids are the repositories and carriers of information.
• All the information needed to make living things work is contained in nucleic
acids
• Nucleic acids also transmit the information needed to make living things work
• Nucleic acids are the basis of protein diversity andbiological diversity.
• The information contained in the DNA makes organisms what they are.
• DNA and RNA are both
polymers of nucleotides
• Nucleotides all have a central
5-carbon sugar, a nitrogenous
base, and a phosphate group.
• The sugar differs between
DNA and RNA.
• RNA uses ribose. DNA uses
deoxyribose.
• The two sugars differ in the
position of 2nd carbon
• The nitrogenous bases
found in DNA are
Adenine, Thymine,
Guanine and Cytosine.
(A,T,G,C)
• The nitrogenous bases
found in RNA are
Adenine, Uracil,
Guanine, and Cytosine.
(A,U,G,C)
• The linkage between nucleotides
is called a phosphodiester bond.
• The sugars are oriented from their
5th carbon to their 3rd carbon.
• The entire polymer has a 5’ to 3’
orientation
• The bases extend from the side of
the polymer
• Both DNA and RNA are
synthesized by adding new
nucleotides to the 3’ end of the
chain.
• RNA is a single stranded polymer
of nucleotides
• DNA is a double stranded
molecule. The two strands coiled
around each other, to form double
helical structure.
• The two strands of DNA run in
opposite directions. They are
compliment to each other.
• Adenine always binds with
Thymine
• Guanine always binds with
Cytosine
• This base pair binding was
explained in Chargaff’s rule.
BIOMOLECULES.pdf
BIOMOLECULES.pdf
THANK YOU

More Related Content

PPT
General biochemistry
PPTX
Ap bio ch 3 Functional Groups & Macromolecules
PPT
Biochemistry lecture 1
PPT
Biological Molecules Notes
PPT
Introduction to biological molecules
PPTX
3. biological macromolecules, bio 101
PPTX
Biomolecules
PPTX
Biomolecules and biochemical reactions
General biochemistry
Ap bio ch 3 Functional Groups & Macromolecules
Biochemistry lecture 1
Biological Molecules Notes
Introduction to biological molecules
3. biological macromolecules, bio 101
Biomolecules
Biomolecules and biochemical reactions

What's hot (19)

PPTX
Baisc biomolecules
PPTX
Biochemistry, Biomolecules and Cell: An Introduction
PPTX
Biomolecules
PPTX
Carbon and Carbohydrates
PPTX
Proteins
PPTX
Organic compounds presentation
PPTX
Biomolecules
PPTX
Carbohydrates
DOCX
Biochemistry
PDF
Chem 45 Biochemistry: Stoker chapter 18 Introduction – Cell Structure
PPT
Cell and macromolecules
PPTX
1.4 lipids UEC Senior 1 Biology 独中高一生物
PPTX
Biomolecules
PPTX
The chemistry of life chapter 3
PPT
Macromolecules in cells
PPTX
Macromolecules and enzymes ppt notes
PPTX
Structure of proteins and nature of bond linking monomers in a polymer
PPTX
Biotechnology:Biomolecules
PDF
3 - Chemical Composition of the Cell - Part 2
Baisc biomolecules
Biochemistry, Biomolecules and Cell: An Introduction
Biomolecules
Carbon and Carbohydrates
Proteins
Organic compounds presentation
Biomolecules
Carbohydrates
Biochemistry
Chem 45 Biochemistry: Stoker chapter 18 Introduction – Cell Structure
Cell and macromolecules
1.4 lipids UEC Senior 1 Biology 独中高一生物
Biomolecules
The chemistry of life chapter 3
Macromolecules in cells
Macromolecules and enzymes ppt notes
Structure of proteins and nature of bond linking monomers in a polymer
Biotechnology:Biomolecules
3 - Chemical Composition of the Cell - Part 2
Ad

Similar to BIOMOLECULES.pdf (20)

PPTX
Water and Biomolecules
PPT
The chemical_basis_for_life---organic_compounds
PPTX
Water and life substances
PPTX
Biomolecules.pptxBiomolecules.pptxBiomolecules.pptx
PPT
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS (1).ppt
PPT
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS.ppt
PPT
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS.ppt
PPTX
Water and life substances
PPTX
Chapter 3 The Organic Molecules of Life
PPTX
BIOMOLECULES_CLASS 11 PRIYA JHA KVS.pptx
PPT
Molecules of life
PPTX
Introduction to basic chemistry of biomolecules
PPTX
Human Physiology Biochemicals
PPT
2. biomolecule
PPTX
1. Basic chemist of Biomolecule (1).pptx
PPT
Bio 100 Chapter 3
PDF
2-180810154111.pdf
PPTX
Biomolecule Examples
PPT
Macromolecules
PDF
biological molecules.pdf
Water and Biomolecules
The chemical_basis_for_life---organic_compounds
Water and life substances
Biomolecules.pptxBiomolecules.pptxBiomolecules.pptx
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS (1).ppt
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS.ppt
7b. The Chemical Basis for Life---ORGANIC COMPOUNDS.ppt
Water and life substances
Chapter 3 The Organic Molecules of Life
BIOMOLECULES_CLASS 11 PRIYA JHA KVS.pptx
Molecules of life
Introduction to basic chemistry of biomolecules
Human Physiology Biochemicals
2. biomolecule
1. Basic chemist of Biomolecule (1).pptx
Bio 100 Chapter 3
2-180810154111.pdf
Biomolecule Examples
Macromolecules
biological molecules.pdf
Ad

Recently uploaded (20)

PPT
Cell Structure Description and Functions
PPTX
Preformulation.pptx Preformulation studies-Including all parameter
PPTX
gene cloning powerpoint for general biology 2
PDF
Cosmology using numerical relativity - what hapenned before big bang?
PPT
Mutation in dna of bacteria and repairss
PPTX
Cells and Organs of the Immune System (Unit-2) - Majesh Sir.pptx
PPTX
Presentation1 INTRODUCTION TO ENZYMES.pptx
PDF
CuO Nps photocatalysts 15156456551564161
PDF
Communicating Health Policies to Diverse Populations (www.kiu.ac.ug)
PDF
Worlds Next Door: A Candidate Giant Planet Imaged in the Habitable Zone of ↵ ...
PDF
BET Eukaryotic signal Transduction BET Eukaryotic signal Transduction.pdf
PPTX
2currentelectricity1-201006102815 (1).pptx
PPTX
SCIENCE 4 Q2W5 PPT.pptx Lesson About Plnts and animals and their habitat
PDF
7.Physics_8_WBS_Electricity.pdfXFGXFDHFHG
PDF
Integrative Oncology: Merging Conventional and Alternative Approaches (www.k...
PPTX
GREEN FIELDS SCHOOL PPT ON HOLIDAY HOMEWORK
PDF
Unit 5 Preparations, Reactions, Properties and Isomersim of Organic Compounds...
PPTX
perinatal infections 2-171220190027.pptx
PDF
From Molecular Interactions to Solubility in Deep Eutectic Solvents: Explorin...
PPTX
gene cloning powerpoint for general biology 2
Cell Structure Description and Functions
Preformulation.pptx Preformulation studies-Including all parameter
gene cloning powerpoint for general biology 2
Cosmology using numerical relativity - what hapenned before big bang?
Mutation in dna of bacteria and repairss
Cells and Organs of the Immune System (Unit-2) - Majesh Sir.pptx
Presentation1 INTRODUCTION TO ENZYMES.pptx
CuO Nps photocatalysts 15156456551564161
Communicating Health Policies to Diverse Populations (www.kiu.ac.ug)
Worlds Next Door: A Candidate Giant Planet Imaged in the Habitable Zone of ↵ ...
BET Eukaryotic signal Transduction BET Eukaryotic signal Transduction.pdf
2currentelectricity1-201006102815 (1).pptx
SCIENCE 4 Q2W5 PPT.pptx Lesson About Plnts and animals and their habitat
7.Physics_8_WBS_Electricity.pdfXFGXFDHFHG
Integrative Oncology: Merging Conventional and Alternative Approaches (www.k...
GREEN FIELDS SCHOOL PPT ON HOLIDAY HOMEWORK
Unit 5 Preparations, Reactions, Properties and Isomersim of Organic Compounds...
perinatal infections 2-171220190027.pptx
From Molecular Interactions to Solubility in Deep Eutectic Solvents: Explorin...
gene cloning powerpoint for general biology 2

BIOMOLECULES.pdf

  • 1. BIOMOLECULES SRIRAMAKRISHNAN.E I M.Sc. Biotechnology Department of Biotechnology and Microbiology National College (Autonomous), Trichy, Tamil Nadu, India
  • 2. The major classes of biological molecules that are important for all living organisms are • carbohydrates • Lipids • proteins • Nucleic acids
  • 3. CARBOHYDRATES • Carbohydrates - compounds that are made of C, H, and O • Examples: all sugars, starches, cellulose and chitin are Carbohydrates used for energy storage and structures. • Carbohydrates have a caloric value of 4.1 kilocalories/gram.
  • 4. • The simplest class of carbohydrates are monosaccharides - simple sugars- All have 3 to 6 carbons
  • 5. • 6 carbon sugars
  • 6. Simple sugars exist in different forms and can be drawn in different ways
  • 7. • The six carbon sugars all have the same chemical formula: C6H12O6 • They differ in the placement of functional groups C=O and -OH • Isomers have the same chemical formula . • Stereoisomers differ in the arrangement of a functional group at a single carbon
  • 8. • Monosaccharides are the building blocks of more complex carbohydrates • For example. Sucrose and lactose are a combination of two monosaccharides
  • 9. • Disaccharides are formed by GLYCOSIDIC linkage by the removal of water molecule
  • 10. • Polysaccharides are polymers of monosaccharides. • Polymers are long chain molecules with repeating subunits • Starches are polymers of glucose • Each glucose molecule is an energy rich molecule • Amylose is an unbranched chain and is produced by plants. Amylopectin is branched and also produced by plants. • Glycogen is highly branched and produced by animals
  • 11. • Starch is a polymer of α- glucose and it is readily soluble • Cellulose is a β-glucose and indigestible • Cellulose is a structural polysaccharide and used for construction of cell wall synthesis by plants. • Another important polysaccharide is chitin which is made up of β-glucose molecule that have nitrogen containing functional group. • chitin is used for the construction of cell wall in fungi.
  • 12. LIPIDS • Lipids - a chemically diverse class of organic molecules that are grouped together because they are all largely nonpolar. • Because they are nonpolar in nature they are soluble in organic solvents like chloroform, benzene, acetone, paint thinner, etc. and insoluble in water • The major classes of lipids are fatty acids, neutral fats, phospholipids, steroids • Lipids have many functions including energy storage, cell membrane structure, vitamins and hormones
  • 13. Saturated fatty acid Unsaturated fatty acid • Fatty acids are long-chain carbon molecules with many carbon- hydrogen bonds and a carboxyl group (COOH) on one end. • The carboxyl group can ionize, releasing an H+ • Saturated fatty acids have no C=C bonds - all carbons in the chain are bonded to as many hydrogens as possible • Unsaturated fatty acids have some C=C bonds in the chain - the carbon chain is not completely saturated with hydrogens.
  • 14. • Phospholipids - structural lipids - an integral part of cell membranes - inside and enclosing cells. • Structurally similar to triglycerides - one fatty acid is replaced by a choline group. • The choline group has both N and P in its structure • The choline group is charged (polar) and will hydrogen bond with water. It is called hydrophilic . • The rest of the molecule is nonpolar and insoluble in water. It will not hydrogen bond with water. It is hydrophobic.
  • 15. • The choline end of the molecule is called the “head.” • The fatty acid chains are called the “tails.” • Phospholipids have hydrophilic heads and hydrophobic tails • In water, phospholipids spontaneously form micelles or bilayers
  • 17. • Steroids or Sterols - have a more complex structure than other lipids and a greater diversity of functions • Cholesterol is an important part of cell membranes • Vitamin D is necessary for some biochemical reactions to occur properly Vitamin D
  • 18. PROTEINS • Proteins – the most functionally diverse class of biological molecules - Protein diversity is the basis of the diversity of life. • Everything that organisms are composed of - all parts - are made of, or by proteins • Proteins serve as enzymes, for defense, transport, support, motion, regulation, and storage • There are 20 different amino acids used in proteins. All have a similar structure. • All have a central carbon, an amino group (NH2) and a carboxyl group (COOH).
  • 19. • Proteins are polymers of amino acids joined through peptide bonds. • The carboxyl group (COOH) of one amino acid links with the amino group (NH2) of another to produce the sequence CONH and release water forms a peptide bond (H2O)
  • 21. • The diversity of protein function results from diversity ofprotein structure which is the result of variation in the sequence of amino acids • Functional proteins can vary in length from about 50 aminoacids to several thousand amino acids • The variety of amino acid sequences that are possible for proteins is practically infinite. • The diversity of amino acid sequence results in diversity of protein structure Protein structure can be classified at several different levels: primary, secondary, tertiary, and quaternary.
  • 22. • Primary structure - the amino acid sequence by the polypeptide bonds • Met - Gly - His - Trp - Lys - ... • Secondary structure - the regular coiling and bending of the polypeptide that results from hydrogen bonding of amino and carboxyl groups in different amino acids. • This forms have 2 characteristic structures - the a helix and the b-pleated sheet
  • 23. • R groups of different amino acids can interact in a variety of ways to produce more complex structure • Hydrogen bonds are weak interactions between polar R groups • Some R groups form covalent bonds or ionic bonds • Nonpolar R groups can have a weak attractive interaction • Because nonpolar R groups are hydrophobic they are found in the interior of proteins
  • 24. • Tertiary structure - the bending and folding of the polypeptide in 3-D space due to the interactions of the R groups distant amino acids • Interactions include: bonding, ionic bonding, covalent bonds, hydrophobic interactions, hydrophilic interactions • Quaternary structure - the interaction of different polypeptides • Quaternary structure is the result of the same interactionsas above. • Not all proteins have quaternary structure
  • 25. • Protein structural diversity is responsible for the functional diversity of proteins. • Protein shape causes protein function • Small changes in shape can influence function • Proteins are sensitive to environmental changes. • Change in pH, temperature, ion concentration can all cause a change in the shape of the protein and influence its functional properties • High temperatures result in weakening of H-bonds. • Proteins tend to denatures (unfold) at high temperature. • Low temperatures strengthen H-bonds. • Proteins become rigid at low temperature.
  • 26. NUCLEIC ACID • Nucleic acids - nucleic acids are the repositories and carriers of information. • All the information needed to make living things work is contained in nucleic acids • Nucleic acids also transmit the information needed to make living things work • Nucleic acids are the basis of protein diversity andbiological diversity. • The information contained in the DNA makes organisms what they are.
  • 27. • DNA and RNA are both polymers of nucleotides • Nucleotides all have a central 5-carbon sugar, a nitrogenous base, and a phosphate group. • The sugar differs between DNA and RNA. • RNA uses ribose. DNA uses deoxyribose. • The two sugars differ in the position of 2nd carbon
  • 28. • The nitrogenous bases found in DNA are Adenine, Thymine, Guanine and Cytosine. (A,T,G,C) • The nitrogenous bases found in RNA are Adenine, Uracil, Guanine, and Cytosine. (A,U,G,C)
  • 29. • The linkage between nucleotides is called a phosphodiester bond. • The sugars are oriented from their 5th carbon to their 3rd carbon. • The entire polymer has a 5’ to 3’ orientation • The bases extend from the side of the polymer • Both DNA and RNA are synthesized by adding new nucleotides to the 3’ end of the chain.
  • 30. • RNA is a single stranded polymer of nucleotides • DNA is a double stranded molecule. The two strands coiled around each other, to form double helical structure. • The two strands of DNA run in opposite directions. They are compliment to each other. • Adenine always binds with Thymine • Guanine always binds with Cytosine • This base pair binding was explained in Chargaff’s rule.