[Illinois] ECE 416 Bio Structure/Function I

By Brian Cunningham

Electrical and Computer Engineering, University of Illinois at Urbana-Champaign, Urbana, IL

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Abstract

           In this lecture, we are given the structure of the protein, its function, role and potentials to the field of biosensors. The parts of the amino acids that make up the proteins are discussed along with bonds and reactions in order to connect these monomers. The structure of the protein is also given through the four levels that develop the protein: Primary, Secondary, Tertiary, and Quaternary structures. Connecting this back to biosensors, each protein has a specific shape due to the amino acid pattern. This shape allows it to make a relationship with specific substrates which on the biosensor surface can help to catch the specific molecules possible. This focuses on the selectivity aspect of the biosensor. Antibodies are also discussed and their potential roles in the selectivity of biosensors.

Cite this work

Researchers should cite this work as follows:

  • Brian Cunningham (2013), "[Illinois] ECE 416 Bio Structure/Function I," https://nanohub.org/resources/16715.

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Time

Location

University of Illinois at Urbana-Champaign, Urbana, IL

Submitter

NanoBio Node, Obaid Sarvana, George Daley

University of Illinois at Urbana-Champaign

Tags

[Illi[Illinois] ECE 416 Lecture 7: Biomolecular Structure and Function I
  • Lesson 5: Proteins 1. Lesson 5: Proteins 0
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  • Amino Acids 2. Amino Acids 166.82471422795604
    00:00/00:00
  • Amino Acids 3. Amino Acids 255.5371779321498
    00:00/00:00
  • Peptide 4. Peptide 294.85058992171133
    00:00/00:00
  • Amino Acids 5. Amino Acids 311.11111111111109
    00:00/00:00
  • Peptide 6. Peptide 351.96824346675493
    00:00/00:00
  • Hydrophylic Amino Acids 7. Hydrophylic Amino Acids 425.14058881905396
    00:00/00:00
  • Hydrophylic Amino Acids 8. Hydrophylic Amino Acids 627.05921270261331
    00:00/00:00
  • Hydrophobic Amino Acids 9. Hydrophobic Amino Acids 667.813430367185
    00:00/00:00
  • Hydrophobic Amino Acids 10. Hydrophobic Amino Acids 845.6500165398611
    00:00/00:00
  • Chain Formation 11. Chain Formation 863.14551402212669
    00:00/00:00
  • The Peptide Bond 12. The Peptide Bond 954.3279303120521
    00:00/00:00
  • 4 Levels of Protein Structure 13. 4 Levels of Protein Structure 992.92093946410853
    00:00/00:00
  • 4 Levels of Protein Structure 14. 4 Levels of Protein Structure 1064.9612232146139
    00:00/00:00
  • α helix 15. α helix 1173.8449663689491
    00:00/00:00
  • β sheet 16. β sheet 1306.399088469879
    00:00/00:00
  • 4 Levels of Protein Structure 17. 4 Levels of Protein Structure 1417.1352960635131
    00:00/00:00
  • 4 Levels of Protein Structure 18. 4 Levels of Protein Structure 1554.6293233359063
    00:00/00:00
  • Protein Interactions 19. Protein Interactions 1664.0276399456022
    00:00/00:00
  • Protein Folding/Unfolding 20. Protein Folding/Unfolding 1774.6609328481641
    00:00/00:00
  • Functional Design of Proteins 21. Functional Design of Proteins 1869.9599367809756
    00:00/00:00
  • Functional Design of Proteins 22. Functional Design of Proteins 1934.2816187010696
    00:00/00:00
  • Functional Design of Proteins 23. Functional Design of Proteins 2045.0178262947038
    00:00/00:00
  • Affinity Constant 24. Affinity Constant 2119.5280626309404
    00:00/00:00
  • Protein-Protein: Pig-IgG on Protein-A 25. Protein-Protein: Pig-IgG on Pr… 2386.5916859631711
    00:00/00:00
  • Protein-Protein Binding 26. Protein-Protein Binding 2670.5333186312346
    00:00/00:00
  • Antibodies (Ab) 27. Antibodies (Ab) 2689.6754511706545
    00:00/00:00
  • Antibody 28. Antibody 2773.8596684676736
    00:00/00:00