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BMS 300: Lipid and protein structure

by: Caroline Hurlbut

BMS 300: Lipid and protein structure BMS 300

Marketplace > Colorado State University > Biomedical Sciences > BMS 300 > BMS 300 Lipid and protein structure
Caroline Hurlbut
GPA 3.7
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About this Document

Main properties of water, phospholipids, and the structures of proteins
Principles of Human Physiology
John P Walrond
Class Notes
Biomedical Science, Physiology




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This 2 page Class Notes was uploaded by Caroline Hurlbut on Saturday August 27, 2016. The Class Notes belongs to BMS 300 at Colorado State University taught by John P Walrond in Fall 2016. Since its upload, it has received 5 views. For similar materials see Principles of Human Physiology in Biomedical Sciences at Colorado State University.

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Date Created: 08/27/16
• water is liquid between 0˚C (freezing point) and 100˚C (boiling point) —distribution of charges or dipole moment makes water liquid at room temp —H atoms have partial positive charge, O atom has partial negative charge —H is hydrogen bonded to other water molecules—>forms matrix of positive charges and negative charges that allows water to interact with each other —in a glass, water interacts with the glass and with other water molecules, held by surface tension • NaCl crystal in water —Na+ and Cl- ions will eventually be liberated from the crystal and be equally distributed in the water column (equilibrium)—>hydrophilic • diffusion across barrier —ion selective channels allow for certain ions to pass through barrier —ions diffuse through channels until concentration on both sides of barrier is equal • aquaporins are water channels —hydrostatic pressure is the downward force of gravity on water —osmotic pressure is the pressure needed on a solution to prevent the flow of water across a membrane —equilibrium eventually reached between these pressures • triglycerides (ex. oil) insoluble in water, lack of charge makes them hydrophobic • glycerol molecule H H removed H C—OH OH = alcohol —> O—C—C—C = ester bond H C—OH H C—OH H • phospholipids —charged phosphate head group and 2 fatty acid side chains—>amphipathic —head group can be one of 3 kinds of molecules A. chocine B. serine C. ethanolamine —interactions with water A. first form: hydrophilic heads face water, hydrophobic tails face air on surface second form: unstable micelle, where heads face outward and tails face B. inward in a sphere C. third form: stable spherical bilayer of phospholipids called liposome D. fourth form: planar phospholipid bilayer (basis of all biological membranes) —mosaic model of biological membranes: phospholipid bilayer with embedded transmembrane proteins to allow charged molecules to pass through hydrophobic region • proteins are amino acid polymers —amino acid structure A. amine group (NH2) B. carboxyl group (COOH) C. variable R group (can be charged or uncharged, 20 possible R groups) —amino acids held together by peptide bonds —chains have amino terminus end and carboxyl terminus end • protein structures —primary structure is the amino acid sequence —secondary structures derived from hydrogen bonding between amine hydrogens and carbonyl oxygen A. alpha helix: interactions within single strand B. beta pleated sheet: interactions between strands —tertiary structure dependent on R groups—>determines protein function • 20 amino acids can be subdivided into 3 categories —non polar—>hydrophobic —polar—>hydrophilic —charged—>hydrophilic • beta sheets can have a parallel or antiparallel organization • tertiary structure is the 3D structure of proteins and determines the protein’s function —folds create binding pockets where R groups can interact with each other —overall shape of protein determined by organization of R groups


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