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BIOLOGY FOR ENGINEERING
APPLICATIONS
Maheswaran Easwaran
Assistant Professor (Sr. G)
Department of Biomedical Engineering
• Genetics
• Bio molecules
• Biological Applications in
Engineering
• Nervous System
GENETICS AND BIO-MOLECULES (Basics only)
 Basics of Genes
 DNA structure
 Genes and hereditary
 Genetic Code
Coding and decoding
Genetic information
 Gene Mapping
 Gene Interactions
 Mutations
 Genetic disorders
 Gene therapy
Basics of Gene
Genetics
• Field of biology
• Study - how traits are passed
• basic components of genetics
• DNA/RNA
• Hold all the genetic information
• Diagnose, treat, prevent and cure many illnesses.
What are Genes?
• In 1865, Gregor Mendal - describe the
elements of heredity.
• Greek - ‘to become’ or ‘to grow into’.
• Genes, which are made up of DNA, acts as
RNA instructor to make molecules - Proteins.
The central dogma of molecular biology
two-step process - transcription and translation
DNA → RNA → protein.
Flow of genetic information
• The lettersA, G, T and
C correspond to the
nucleotides found in
DNA.
• organized into codons.
• Collection of
codons - Genetic
code.
• 20 amino acids
• Codon - 3 nucleotides
Genetic Code
• Set of rules used by living cells
• To translate information
• Encoded within genetic material into
proteins
Genetic Code
Initiator codon
⚫AUG is the initiator codon in majority
of proteins
⚫In a few cases GUG may be the
initiator codon
⚫Methionine is the only amino acid
specified by just one codon,AUG.
Non Sense Codons
⚫ 3 codons - 64 in genetic code
⚫ Termination codons or stop codons
⚫ nonsense codons
⚫ UAA, UAG, and UGA.
⚫ No amino acid.
⚫ The ribosome pauses
Non Sense Codons
Clinical Significance
⚫Mutations can be well explained using
the genetic code.
Mutations
1) Silent
2)Misense
3)Nonsense
Frameshift
Silent Mutations
Single nucleotide change-Ato G, same
amino acid is incorporated. Mutation goes
unnoticed.
Missense mutations
Single nucleotide change A to C – different amino
acid incorporated. Loss of functional capacity of
protein.
Non sense Mutation
Single nucleotide change from C to T, stop codon is
generated (In m RNA represented by UAG), premature
termination of chain, may be incompatible with life.
Frame sift Mutations
⚫ Insertion or removal of a base/bases can alter the
reading frame with the resultant incorporation of
different amino acids
CARBOHYDRATES
Carbohydrates:
Fatty acids
Nucleic Acids
Introduction:
• Large biomolecules
• Essential – life
• Bac, Virus., Mitocon.,
• Encode and Store information
• Express – information
PROTEIN
Central dogma of molecular biology
Translation (inside the
ribosome (with help of
tRNA):
Translation: making a
peptide using mRNA as
the coding template
(peptide synthesis)
mRNA… messenger RNA
tRNA … transfer RNA
mRNA
The structure of proteins
1° structure: Amino acid sequence
–Twenty amino acids common to all organisms.
–Each has amino group, carboxyl group, R group
and a hydrogen
–Linked together by peptide bond.
The structure of
proteins
Alpha helix:
- right-handed helix
-100° rotation (twist)
- 3.6 residues/turn
-stabilized by H-bonds
between NH and CO group
(four residues up).
2° structure: alpha helix
-helix
(© by Irvine Geis)
Biochemistry Voet & Voet
Red – oxygen
Black – carbon
Blue – nitrogen
Purple – R-group
White – C
Hydrogen-bonds between C-O of nth
and N-H group of n+4th residue.
PHYSICAL PROPERTIES OF PROTEINS
Protein solutions exhibit colloidal properties
Molecular weights
Insulin (5,700); Hemoglobin (68,000);
Albumin (69,000); Immunoglobulins (1,50,000)
Shape: Insulin is globular, Albumin is oval in shape,
Fibrinogen molecule is elongated.
Classification Based on Functions
1. Catalytic proteins, e.g. enzymes
2. Structural proteins, e.g. collagen, elastin
3. Contractile proteins, e.g. myosin, actin.
4. Transport proteins, e.g. hemoglobin, albumin, transferrin
5. Regulatory proteins or hormones, e.g. ACTH, insulin
6. Genetic proteins, e.g. histones
7.Protective proteins, e.g. immunoglobulins, interferons,
Clotting factors.
Thank you!

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Biology for Engineering Applications Mod 3 (2).pptx

  • 1. BIOLOGY FOR ENGINEERING APPLICATIONS Maheswaran Easwaran Assistant Professor (Sr. G) Department of Biomedical Engineering
  • 2. • Genetics • Bio molecules • Biological Applications in Engineering • Nervous System
  • 3. GENETICS AND BIO-MOLECULES (Basics only)  Basics of Genes  DNA structure  Genes and hereditary  Genetic Code Coding and decoding Genetic information  Gene Mapping  Gene Interactions  Mutations  Genetic disorders  Gene therapy
  • 5.
  • 6.
  • 7. Genetics • Field of biology • Study - how traits are passed • basic components of genetics • DNA/RNA • Hold all the genetic information • Diagnose, treat, prevent and cure many illnesses.
  • 8. What are Genes? • In 1865, Gregor Mendal - describe the elements of heredity. • Greek - ‘to become’ or ‘to grow into’. • Genes, which are made up of DNA, acts as RNA instructor to make molecules - Proteins.
  • 9.
  • 10.
  • 11. The central dogma of molecular biology two-step process - transcription and translation DNA → RNA → protein. Flow of genetic information
  • 12. • The lettersA, G, T and C correspond to the nucleotides found in DNA. • organized into codons. • Collection of codons - Genetic code. • 20 amino acids • Codon - 3 nucleotides
  • 13. Genetic Code • Set of rules used by living cells • To translate information • Encoded within genetic material into proteins
  • 15.
  • 16. Initiator codon ⚫AUG is the initiator codon in majority of proteins ⚫In a few cases GUG may be the initiator codon ⚫Methionine is the only amino acid specified by just one codon,AUG.
  • 17. Non Sense Codons ⚫ 3 codons - 64 in genetic code ⚫ Termination codons or stop codons ⚫ nonsense codons ⚫ UAA, UAG, and UGA. ⚫ No amino acid. ⚫ The ribosome pauses
  • 19.
  • 20. Clinical Significance ⚫Mutations can be well explained using the genetic code. Mutations 1) Silent 2)Misense 3)Nonsense Frameshift
  • 21. Silent Mutations Single nucleotide change-Ato G, same amino acid is incorporated. Mutation goes unnoticed.
  • 22. Missense mutations Single nucleotide change A to C – different amino acid incorporated. Loss of functional capacity of protein.
  • 23. Non sense Mutation Single nucleotide change from C to T, stop codon is generated (In m RNA represented by UAG), premature termination of chain, may be incompatible with life.
  • 24. Frame sift Mutations ⚫ Insertion or removal of a base/bases can alter the reading frame with the resultant incorporation of different amino acids
  • 27.
  • 28.
  • 29.
  • 30.
  • 31.
  • 32.
  • 33.
  • 35.
  • 36.
  • 37.
  • 38.
  • 40. Introduction: • Large biomolecules • Essential – life • Bac, Virus., Mitocon., • Encode and Store information • Express – information
  • 41.
  • 42.
  • 43.
  • 44.
  • 45.
  • 46.
  • 48. Central dogma of molecular biology Translation (inside the ribosome (with help of tRNA): Translation: making a peptide using mRNA as the coding template (peptide synthesis) mRNA… messenger RNA tRNA … transfer RNA mRNA
  • 49.
  • 50.
  • 51.
  • 52.
  • 53. The structure of proteins 1° structure: Amino acid sequence –Twenty amino acids common to all organisms. –Each has amino group, carboxyl group, R group and a hydrogen –Linked together by peptide bond.
  • 54. The structure of proteins Alpha helix: - right-handed helix -100° rotation (twist) - 3.6 residues/turn -stabilized by H-bonds between NH and CO group (four residues up). 2° structure: alpha helix -helix (© by Irvine Geis) Biochemistry Voet & Voet Red – oxygen Black – carbon Blue – nitrogen Purple – R-group White – C Hydrogen-bonds between C-O of nth and N-H group of n+4th residue.
  • 55. PHYSICAL PROPERTIES OF PROTEINS Protein solutions exhibit colloidal properties Molecular weights Insulin (5,700); Hemoglobin (68,000); Albumin (69,000); Immunoglobulins (1,50,000) Shape: Insulin is globular, Albumin is oval in shape, Fibrinogen molecule is elongated.
  • 56. Classification Based on Functions 1. Catalytic proteins, e.g. enzymes 2. Structural proteins, e.g. collagen, elastin 3. Contractile proteins, e.g. myosin, actin. 4. Transport proteins, e.g. hemoglobin, albumin, transferrin 5. Regulatory proteins or hormones, e.g. ACTH, insulin 6. Genetic proteins, e.g. histones 7.Protective proteins, e.g. immunoglobulins, interferons, Clotting factors.