Week 4 - "Proteins"

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Proteins

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70 Terms

1

Proteins

Naturally occurring and branch of monomer unit; amino acids; they account for 15% of all a cell's overall mass

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2

Proteins

Responsible for moving substances such as nutrients and electrolytes across the membrane; hormones and neurotransmitter

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3

Proteins

Ack as markers; process by which different cells recognize each other

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4

9000

________ different kinds of proteins in a typical human cell

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5

100,000

Number of different proteins found within the human body

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6

Proteins

Needed for the synthesize of enzymes, certain hormones and some blood component; maintenance, repair of existing tissues and synthesis of new one

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7

Carbon, Hydrogen, Oxygen and nitrogen

All proteins contain the elements _____________ (4) almost all contain sulfur

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8

15.4%

The average nitrogen proteins is _______ by mass

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9

Amino acids

Contain both amino and carboxyl groups attached to the same carbon atom; building blocks for proteins

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10

R-Groups

Non polar amino acids are _______

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11

Polar Neutral

Contains polar but neutral side chains; 7 amino acids

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12

Polar Acidic

Contains carboxyl as a part of side chains; 2 amino acids

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13

Polar Basic

Contains amino group as part of the side chains; 2 amino acids

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14

Casein

Main protein of milk (phosphorus); important diet of infants and children

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15

Hemoglobin

Oxygen transporting protein of blood; Iron

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16

Alanine, Cystein, Glycine

Non Polar examples (first 3 lang nandito pero madami yun)

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17

Arginine, Asparagine, Aspartic Acid

Polar examples (first 3 lang nandito pero madami yun)

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18

Polar Amino Acid

Oppositely charged; electron is not evenly distributed in the molecule can cause a "dipole mole"

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19

Dipole mole

One end of the molecule is positive while the other is negative

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20

Non-polar

Equally charged amino acid

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21

Cystein

Unique sulfhydryl group; Non essential amino acid. Nails, skin and hair and for collagen making

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22

Peptide

Short chain amino acid; it build muscle, boost weight and muscle recovery

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23

Peptide Bond

Covalently bonded between amino acids

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24

Dipeptide Bond

Covalently bonded between 2 amino acids

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25

Oligopeptide

Covalently bonded between 10-20 amino acids

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26

Polypeptide

Covalently bonded between many amino acids

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27

Isomeric Peptides

Same amino acid but different order and are of different molecules with different property

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28

Hormonal action, neurotransmission, antioxidant activity

Biochemically important peptides

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29

Oxytocin and Vasopressin

Best known peptide hormone; made by pituitary glands

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30

Vasopressin

Lactation, water balance, and skeletal integral

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31

Oxytocin

Uterine contraction, breast tissue for lactation after birth.

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32

Enkephalin

Small peptide neurotransmitter

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33

Met-Enkephalin, Leu enkephalin

Help reduces pain; produced by the brain and bind receptors

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34

Glutathione

Small Antioxidant; known for whitening but also serve as regulation of oxidation, protects cellular component from oxidation of peroxide and superoxide

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35

Simple protein

Amino acid residue is present

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36

Conjugated protein

One or more amino acid residue are present

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37

Lipoprotein

Lipids prosthetic groups

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38

Glycoprotein

Carbohydrate groups

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39

Metalloprotein

Specific metal as prosthetic groups

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40

10,000

Count of Amino acid residue known

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41

400-500

Common proteins contain ______ to _______ amino acid residue

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42

40-100

Small proteins contain _____ to ____ amino acid residue

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43

Monomeric

Contains one peptide chain

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44

Multimeric

Contains more than one peptide chain

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45

Primary structure

Order in which amino acids are linked together in a protein

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46

Frederick Sanger (1953)

First to sequence and determine the primary structure for the first protein; Insulin

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47

Secondary Structure

Arrangement of atoms of backbone in space; Alpha-helix and beta-pleated

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48

Alpha-Helix

Adopts the coil like spring shape

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49

Beta-pleated sheets

Completely extended amino acid chains

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50

Tertiary Structure

Three-dimensional shape

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51

Quaternary Structure

organization among the various peptide chains in a multimeric proteins

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52

Fibrous, globular, membrane

Three types of proteins

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53

Fibrous proteins

elongated shaped; generally insoluble in water, linear structure; hair, nails

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54

Globular proteins

Folded into spherical shapes; generally soluble in water; functions as enzymes and intracellular in the protein core

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55

Membrane proteins

Associated with cell membrane; Insoluble in water; helps in transport of molecules the membrane

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56

Alpha-Keratin

Protective coating for organs; protein constituent of hairs, feather and nails

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57

Collagen

30% Most abundant protein; structural material in tendons, ligaments and blood. Rich in proline 20%

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58

Myoglobin

Oxygen storage molecules in muscles; serve as reservoir of oxygen source for working muscles

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59

Hemoglobin

Oxygen carrier molecule in blood; transport oxygen from lungs to tissues. Can transmit up to 4 oxygen molecules

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60

glycoprotein

a conjugated protein having a carbohydrate component

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61

Junction

Serve to connect and join cells together

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62

Enzyme

Fixing membranes; localizing metabolic pathways

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Transport

Helps facilitated and active transport

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Recognition

Marker for cellular identification

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65

Immunoglobulin

Protective response to the invasion of microorganism or foreign molecules

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66

Lipoproteins

Help suspend lipids and transport them into the bloodstream

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67

Chylomicrons

Transport dietary triacylglycerol's from intestine and liver to adipose tissue

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68

Very-low density lipoproteins

Transport triacylglycerol synthesized in the liver to adipose tissues

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69

Low-density lipoproteins

Transport cholesterol synthesized in the liver to cells throughout the body

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70

High-density lipoproteins

Collects excess cholesterol from the body tissue and transport it back to the liver for degradation to bile acids

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