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4.PROTEINS - Coggle Diagram
4.PROTEINS
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POLYPEPTIDES
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PRIMARY STRUCTURE
THE PRIMARY STRUCTURE OF A PROTEIN IS FORMED BY THE POLYPEPTIDE CHAIN THROUGH COVALENT PEPTIDE BONDS
PRIMARY STRUCTURE CONTROLS ALL SUBSEQUENT LEVELS OF ORGANISATION BECAUSE IT DETERMINES THE ANTURE OF THE INTERACTIONS BETWEEN R GROUPS
BECAUSE AMINO ACIDS ARE IN A PRECISE POSITION, CONFORMATION OF THE PROTEIN IS PREDICTABLE AND REPEATABLE
PROTEIN STRUCTURE LEVELS
SECONDARY STRUCTURE
SECONDARY STRUCTURE IS BASED ON HYDROGEN BONDING BETWEEN NON-ADJACENT AMINO ACIDS TO STABILIZE THE ARRANGEMENT
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TERTIARY STRUCTURE
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THIS INCLUDES: H-BONDS, DISULFIDE BONDS BETWEEN CYSTEINES, IONIC BONDS AND HYDROPHOBIC INTERACTIONS
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POLARITY OF AMINO ACIDS
POLAR PROTEINS WILL HAVE NON-POLAR AMINO ACIDS CLUSTERED AT THEIR CORE WHILE POLAR AMINO ACIDS WILL BE ON THE SURFACE
INTEGRAL MEMBRANE PROTEINS HAVE NON-POLAR AMINO ACIDS ON THE SURFACE TO INTERACT WITH FATTY ACID TAILS AND EMBED IN MEMBRANES
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ENVIRONMENTAL EFFECTS
DENATURATION IS A STRUCTURAL CHANGE IN A PROTEIN THAT RESULTS INN THE LOSS OF ITS BIOLOGICAL PROPERTIES
TEMPERATURE
HIGH TEMPERATURES MAY DISRUPT H BONDS THAT HOLD THE PROTEIN TOGETHER, UNFOLDING THE PROTEIN AND LOSE ITS CAPACITY TO FUNCTION
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