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

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Presentation Description

ubio is starting a series of biology tutorials aimed at introducing biology, biotechnology and bioinformatics to computer engineers. The first part of the presentation is essentially a biochemistry tutorial that introduces molecular biochemistry.

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By: Harman (62 month(s) ago)

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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

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Amino Acids Glycine – simplest amino acid (NH2-CH2-COOH)

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Proteins

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Structure of Proteins

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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.

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Secondary Structure Sheet formation Helix formation Each strand in a sheet is represented by a pointed ribbon

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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.

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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)

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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

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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

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In Part 2…

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ubiquitous . biology www.ubio.in