(www.ubio.in) Biology for Computer Engineers Part1

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Information about (www.ubio.in) Biology for Computer Engineers Part1

Published on March 29, 2008

Author: faisal

Source: authorstream.com

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

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