Biologically Important Molecules 1

Front 1

Hydrophobic Amino Acids Def

Back 1

-water fearing, non polar

-found burried in the interior of proteins

-prefer contact with one another over h20

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Name Hydrophobic Alipathic Amino Acids & (ABBR)

Back 2

• glycine (gly)
  
• alanine (ala)
  
• valine (val)
  
• leucine (leu)
  
• Isoleucine (ILE)
  
• Methionine (Met)
  

Front 3

Name Hydrophobic Aromatic Amino Acids (ABBR)

Back 3

• phenylalanine (phe)
  
• proline (pro)
  
• tryptophan (trp)
  

Front 4

3 Subdivisions of Hydrophillic Amino Acids

and their features

Back 4

1) Polar-Neutral

2) Polar- Acidic- Negative

3) Polar - Basic -Positive

-attracted to polar h20

-on surface of proteins

-R-Groups have h20 affinity

Front 5

Name the Polar Acidic Amino Acids & (ABBR)

Back 5

• Aspartate- Aspartic Acid (asp)
  
• Glutamate- Glutamic Acid (glu)
  

Front 6

Name the Polar Neutral Amino Acids (ABBR)

Back 6

• Serine (ser)
  
• Threonine (Thr)
  
• Tyrosine (Tyr)
  
• Cysteine (Cys)
  
• Asparagine (Asn)
  
• Glutamine (Glu)
  

Front 7

Name the Polar Basic Amino Acids (ABBR)

Back 7

• Lysine (Lys)
  
• Arginine (Arg)
  
• Histidine (His)
  

Front 8

Glycine (G) Side Chain Structure

Back 8

Front 9

Alanine (a) Side Chain Structure

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Front 10

Valine (v) Side Chain

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Front 11

Leucine (L) Side Chain Structure

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Front 12

Methionine (M) Side Chain Structure

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Front 13

Isoleucine (I) Side ChainStructure

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Front 14

Phenylalanine (F) Side ChainStructure

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Front 15

Tyrosine (Y) Side Chain & Pka

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Pka=10.07

Front 16

Tryptophan (w) Side Chain Structure

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Front 17

Serine (s) Side ChainStructure

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Front 18

Threonine (T) Side ChainStructure

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Front 19

Cysteine (c) Side Chain & Pka

Back 19

forms disulfide bonds

Pka= 8.0

Front 20

Proline (p) Side Chain Structure

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Front 21

Aspararagine (N) Side Chain Structure

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Front 22

Glutamine (Q) Side Chain Structure

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Front 23

Lysine (K) Side Chain & Pka

Back 23

Pka= 10.53

Front 24

Arginine (R) Side Chain & Pka

Back 24

Pka= 12.48

Front 25

Histidine (H) Side Chain & Pka

Back 25

Pka= 6.10

Front 26

Aspartate- Aspartic Acid-(D) Side Chain & Pka

Back 26

Pka= 3.86

Front 27

Glutamate - Glutamic Acid-(E) Side Chain & Pka

Back 27

Pka= 4.07

Front 28

Peptide Bond (Amide Bond) Formation [Def & Drawing]

Back 28

Amide attacks carboxyl carbon releasing 1 H20

Front 29

Describe the N to C formation of polypeptides

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The N terminal starts a peptide chain, is connected to the left of the alpha carbon, the carboxyl group is connected to the right c-terminal end of the chain

Thus Polypetides Move in the N to C Direction

Front 30

Describe the Primary Structure of Proteins and Primary R Groups

Back 30

Primary structure is the amino acid sequence of protein chain

primary r groups determine folding of protein and final 3-D structure

Front 31

Describe the formation of a Secondary Structure A-Helix

Back 31

initial folding of the protein where hydrogen bonding between the amide hydrogens and carbonyl oxygens of the peptide bonds occur

Front 32

Describe a type of Fibrous protein and how they are formed

Back 32

a-keratins are a type of secondary structure that form a hair cell

1-an a-helix bundles with 2 other helices to form a protofibril

2-many protofibrils combine to form a microfibril (insoluble)

3- tons of microfibrils make a macrofibril making a hair cell

Front 33

Name the two types of secondary structures

Back 33

• a-helix
  
• b-pleated sheet
  

Front 34

Describe a B pleated sheet and the two types of formations

Back 34

all of the carbonyl oxygens and amide hydrogens are involved in boding

• Parallel: if the N termini of one chain is aligned with the N termini of another chain
• Antiparallell: n-terminus is aligned with the c-terminus of another chain
  

Front 35

Describe the formation of Tertiary Structure and their shape?

Back 35

Globular Proteins

further folding of secondary structure 1 chain

Front 36

Name the Tertiary structure side chain forces and describe them

Back 36

1) Van der walls: hold r groups of nonpolar amino acids that are hydrophobic

2) Hydrogen bonds: hydrogen bonds between polar (- to +) H+ to -OR groups

3) Disulfide Bridges: Oxidation of 2 cysteine SH groups to form s-s bond

4) Salt Bridges: ionic bonds between oppositely charged Carboxyl O- and +NH3 Amino groups

5) Covalent bonds of thiol amino acids (aromatics with circles)

Front 37

Describe the formation of Quateranary Structure and the forces that it has

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Multiple polypetide side chains interact to form an activated protein or enzyme

uses the same side chain forces as tertiary structure to hold multiple chains together

Front 38

Describe Carbohydrates and their functions

Back 38

simple sugars

Function: provide an energy source for cellular metabolism because they are easily broken down to co2 via oxidation

Front 39

Name two Complex Carbs

Back 39

starches and cellulose

Front 40

Describe Monnosaccharides and name examples

Back 40

single sugar unit (monomer)

6 Carbon Monosaccharides

• glucose
  
• fructose
  
• galactose
  

5 Carbon Monosaccharide

• Ribose
  
• DeoxyRibose
  

Front 41

Naming Monosaccharides Ketoses and Aldoses

Back 41

Ketose: has a ketone functional group

Aldose: aldehyde functional group

# OF CARBONS

• triose 3
  
• tetrose 4
  
• pentose 5
  
• hexose 6
  

Front 42

Name D-Glucose Isomers and describe their structures

Back 42

A-Glucose has C-1 hydroxyl above ring

B-Glucose has C-1 hydroxyl below ring

Front 43

Describe how Disaccharides are connected and name examples and the monomers that make them

Back 43

two monosaccharides connected via a glycosidic linkage, a Glucose attached to something else

• maltose= glucose + glucose
  
• lactose= glucose + galactose
  
• sucrose= glucose + fructose
  

Front 44

Glycosidic Bonds [Alpha vs Beta] Describe their structures

Back 44

A 1-4 linkages occur when hydroxyl groups on 1 and 4 are both in the beta position (down) makes a v shaped link

B 1-4 linkages occur when hydroxyl groups on 1 and 4 are opposite creating a straight bond

Front 45

Describe the linkages of Maltose

Back 45

made of 2 a-d-glucose molecules with an a 1-4 linkage

Front 46

Describe the linkages of lactose

Back 46

made of one molecule of B-D-Galactose and one of either a or b glucose. b1-4 linkage

Front 47

Describe the linkages of Sucrose

Back 47

water soluble sugar of plants

product of a-d-fructose and b-d-fructose via an a1-->b2 anomeric linkage

Front 48

Describe the different Polysaccharides and their function

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Homopoly: made up of a single monosaccharide

hetero: made up of two or more monosaccharides

1) Glycogen- animal glucose storage

2) Starch- corn plant glucose storage

3) Cellulose- plant structure

Front 49

Glycogen Description and formation

Back 49

storage molecule for glucose, found in the liver and skeletal muscles

made of many glucose molecules connected via a 1-4 and many short glucose side branches connected via a 1-6 linkages

Front 50

Describe the breakdown of Amylose to form Glucose

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amylose is a starch that is broken down by (A Amylase and B Amylase hich cleave maltose off then is converted to glucose via maltase

Front 51

Function of hydrolyzing glycosidic linkages and how they are named

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the hydrolysis of polysaccharides such as maltose into two units of glucose allows glucose to enter metabolic pathways as an energy source

the enzymes that hydrolyze glycosidic bonds are named after the sugar they work on and are highly specific

Front 52

Describe how Polysaccharides regulate the break down of glycogen

Back 52

Because the hydrolyzation of polysacharides requires a high energy of activation it allows us to use enzymes as gate keepers: when we need energy from glucose we open the gate of glycogen hydrolysis

Front 53

Alpha and Beta 1-4 connections disaccahrides

Image

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Front 54

General Amino Acid Structure Image

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Front 55

Proline Unique Features

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unique amino acid, its amino group is covalently bonded to its own side chain creating a secondary alpha amino group and a ring like structure

Front 56

Disulfide Bond Formation Image

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Front 57

Glycogen Bonding Image

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Hydrolysis of Disaccharide Maltose Bond Image

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Alpha Helix Bonding Image

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Front 60

Parallel B pleated Sheet Image

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Front 61

Anti Parallel B-Pleated Sheet Image

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Front 62

Tertiary Structure Image

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