Presentation Transcript
Slide1: Biology For Computer Engineers
Part 1: Chemistry for Biology
Slide2: Why me, the computer geek?
Slide3: What is Biology?
Slide4: Approaches to Biology
Slide5: Composition in Biology
Slide6: Inheritance and Classification
Slide7: Organic Chemistry for Biology
Slide8: Organic Molecules
Slide9: Structure of Organic Molecules
Slide10: Bio-Molecules
Slide11: Amino Acids
Slide12: Amino Acids Glycine – simplest amino acid
(NH2-CH2-COOH)
Slide13: Proteins
Slide14: Structure of Proteins
Slide15: Primary Structure Each bead in the chain is an amino acid.
Amino Acids are represented by 3-letter abbreviations. Upto 20 amino acids are used to make proteins.
Each Amino Acid has unique chemical properties:
Hydrophobic/hydrophilic
Acidic/Basic, etc.
Some Amino Acids can be manufactured by the body. Amino Acids that are not manufactured have to be taken through food. These are Essential Amino Acids.
Slide16: Secondary Structure Sheet formation Helix formation Each strand in a sheet is represented by a pointed ribbon
Slide17: Tertiary Structure A protein secondary structure might be a sequence of sheets and helices. The secondary structure folds in 3-d space due to attractive forces. This creates the tertiary structure.
Slide18: Quaternary Structure Collagen triple helix: There are three polypeptide chains intertwined with each other to form the thread-like collagen structure. Collagen is used to make long muscular tissue like ligaments Haemoglobin consists of 4 polypeptide chains, each containing a heme group (that contains iron, shown in green)
Slide19: Importance of Protein Structure Impact of Primary Structure modification: the curious case of Sickle Cell Anaemia
Amino-acid in position 6 of one of the haemoglobin sub-units is different in people with Sickle Cell Anaemia.
Haemoglobin molecules float around in red blood cells (RBCs). Oxygen binds to them in lungs and unbinds in tissues. This is how tissues receive Oxygen.
In de-oxygenated state, modified haemoglobin molecules stick together to form long chain polymers which then bundle together like a rigid multi-strand braid.
The braid causes affected RBCs to bend like a sickle. They become normal again upon oxygenation.
Repeated change in structure causes rupture and destruction of RBCs
Slide20: Importance of Protein Structure Loss of structure and disease
Loss of structure renders proteins dysfunctional
Functions that depend on the protein are affected
Aggregates might be toxic or might interrupt activity of cells
Examples
Alzheimer’s disease
Parkinson’s disease
Mad Cow disease
This is a major research area
Slide21: In Part 2…
Slide22: ubiquitous . biology www.ubio.in