Anatomy-Lecture Four

Front 1

Protein Structure Organization (4)

Back 1

Primary
Secondary
Tertiary
Quaternary

Front 2

Primary structure (Protein Structure Organization)

Back 2

Unique amino acid sequence makes a polypeptide chain
Not usually a true protein, too simple
Proteins rarely exist in this form!

Front 3

Secondary structure (Protein Structure Organization)

Back 3

-Polypeptide chain twisted or folded
-two types (these help to maintain shape!)

Front 4

What are the two types of Secondary Structure?

Back 4

Alpha Helix
Beta Pleated

Front 5

Tertiary structure (Protein Structure Organization)

Back 5

-Primary & Secondary levels are folded into 3-D shapes
-AA far apart in sequence, brought together so bonds can form

Front 6

Molecular shape is always going to dictate _______.
If you change the shape, you change the ______.
(same answer)

Back 6

function

Front 7

Quaternary structure (Protein Structure Organization

Back 7

-Proteins with more than 1 polypeptide chain are folded and bonded
-Very complex structure

Front 8

(Structural Proteins-Protein Organized by Function)
Also call _______ (1) , (strand like appearance).
Provide tensile ______(2).
Are they soluble? (3)
Chemically very ______(4).

Back 8

1.) Fibrous Proteins
2.) Strength
3.) No, insoluble.
4.) Stable

Front 9

Name three examples of Structural Proteins.

Back 9

Collagen (Bone, Tendon, Ligament, Cartilage)
Keratin (Hair, Nails, Skin)
Elastin

Front 10

(Functional Proteins-Protein Organized by Function)
Also called _____ ______ (1).
Are they soluble? (2)
They can ____ ______ very well (3).

Back 10

1.) Globular Proteins
2.) Yes!
3.) move around

Front 11

Name three examples of Functional Proteins.

Back 11

Antibodies and antigens
Protein based hormones
Enzymes

Front 12

Functional Proteins are chemically ________ (1) and two examples the affect them are ____ and ____ (2).

Back 12

1.) Unstable
2.) Abnormal pH and heat

Front 13

Affecting a functional protein will disrupt hydrogen bonds maintaining all structure types expect _______ ____.

Back 13

Primary Structure

Front 14

All enzymes are proteins, but not all proteins all ______.

Back 14

Enzymes.

Front 15

(Functional Proteins)
When Protein unravels, it is ______.

Back 15

Denatured

Front 16

Functional Proteins are sometimes ______.

Back 16

Reversible.

pH 7.4 7.5 (10% shift)
(Break virtually all hydrogen bonds in proteins
Return to 7.4 = Bonds reform
Protein resume normal structure & function)

Front 17

Functional (Globular) proteins control most ______ (1) reactions in the body and are very sensitive to _____(2) changes.

Back 17

1.) chemical
2.) homeostatic

Front 18

(Functional Proteins)
Enzymes function as biological ____(1), and regulate ______(2) rates, and are Not changed or used up.

Back 18

1.) catalysts
2.) reaction

Front 19

Some enzymes are completely _______.

Back 19

Protein

Front 20

Some enzymes have 2 parts. They are called _____ and ______.

Back 20

Protein part
Cofactor

Front 21

Cofactor

Back 21

Ion of metal/nonprotein partners (iron, copper, zinc, magnesium or calcium ions)
Organic molecule
Essential to function

Front 22

If the cofactor is from a vitamin ( like B complex) the cofactor called a _____.

Back 22

Coenzyme

Front 23

Cofactors bind to ______ and change its shape.

Back 23

Enzymes

Front 24

(Coenzymes)
Organic cofactors derived from ___ ____ (1) vitamins (niacin, riboflavin).
Transfer ______(2) between enzymes.

Back 24

1.) Water-soluble
2.) Electrons

Front 25

"Lysis" means _______ ______.

Back 25

Breaking down

Front 26

Each enzyme is highly specific. It controls a ____(1) reaction or small group of related reactions.

Back 26

1.) Single

Front 27

Enzymes are named according to ______.

Back 27

Substrate

Front 28

Most enzymes end in _____.
Provide an example.

Back 28

-"ase"
-ex: oxidase

Front 29

Chemical reactions require _____ ______(1), and ______(2) are that energy needed to trigger reactions.

Back 29

1.) Activation energy
2.) Enzymes

Front 30

Anything that combines with an enzyme is called a _______.

Back 30

Substrate

Front 31

(Enzymatic Reaction Steps)
Enzyme temporarily binds to ____(1), but is ____(2), and will eventually go back to its ____(3) form. In this the ____(4) bond is broken.

Back 31

1.) Substrate
2.) Unstable
3.) Original
4.) Covalent

Front 32

Enzyme-Substrate Complex

Back 32

Internal rearrangement
Forms new product

Front 33

(Nucleic Acids-Organic Substances)
Large and ______(1) molecules.
Control ____ & _____(2) of entire organism.

Back 33

1.) Complex
2.) Structure & Function

Front 34

Nucleic Acids are composed of _____ elements.

Back 34

Five

Front 35

Name the 5 elements Nucleic Acids are composed of.

Back 35

Carbon
Hydrogen
Oxygen
Nitrogen
Phosphorus

Front 36

What are the 2 kinds of Nucleic Acids?

Back 36

RNA or Ribonucleic Acids
DNA or Deoxyribonucleic Acid

Front 37

_______ are building blocks of Nucleic Acids.

Back 37

Nucleotides

Front 38

What are the three components of Nucleic Acids?

Back 38

-Phosphate group (phosphorus plus oxygen)
-Nitrogenous base (1 of several)
-5 Carbon sugar (Ribose or Deoxyribose)

Front 39

DNA is located in the _____.

Back 39

Nucleus

Front 40

DNA has two roles:
Carry & replicate ______(1) information.
Provide instructions for building _____(2).

Back 40

1.) Genetic
2.) Proteins

Front 41

DNA Structure is also called a _____ _____.

Back 41

-Double Helix or Twisted Ladder

Front 42

A double row of nucleotides in the DNA structure is make up of _____ ______(1) and _____ ______(2).

Back 42

1.) Alternating Phosphate group
2.) Deoxyribose Sugar

Front 43

What are the 4 Nitrogenous Bases attach to Deoxyribose sugar?

Back 43

Adenine
Thymine
Cytosine
Guanine

Front 44

In DNA, what are the complimentary pairs that bond with bases?

Back 44

Adenine – Thymine
Thymine - Adenine
Cytosine - Guanine
Guanine – Cytosine
HINT: AT/GC!

Front 45

Genetic Code results from the order (sequence) that _____ occur.

Back 45

Bases

Front 46

Genetic Code determines ____ _____ to be manufactured.

Back 46

-Amino Acids

Front 47

____(1) bases in a row (triplet) codes for _____(2) Amino Acid.

Back 47

1.) Three
2.) One
Ex: TTT = Lysine
ATA Tyrosine

Front 48

Sequence of Nucleotide Triplets (Amino Acids) direct the formation of _____ protein.

Back 48

One

Front 49

Sequences of DNA structure is called a _____.

Back 49

Gene

Front 50

Gene: segment of a _____ ______ (1) that carries the instructions for making one _____(2), always looking for the next thing that creates the change.

Back 50

1.) DNA molecule
2.) Protein

Front 51

(DNA Structure)
Start & stop Triplets signal (a marker):
Beginning of a Gene is _____ (1).
End of a Gene is ______(2).

Back 51

1.) TAC
2.) ATT

Front 52

RNA stands for ______ _____.

Back 52

Ribonucleic Acid

Front 53

All Ribonucleic Acid is formed in the ____.

Back 53

Nucleus

Front 54

RNA moves into & stay in _____ after formation.

Back 54

Cytoplasm

Front 55

The function of RNA is to carry out orders for ______ synthesis issues by DNA.

Back 55

Protein

Front 56

RNA structure is similar to DNA, except 5 carbon sugar is _________.

Back 56

Ribose

Front 57

The Nitrogenous bases of RNA are: (4)

Back 57

Adenine
Cytosine
Guanine
Uracil

Front 58

RNA has the same bases as DNA except _____
is present instead of Thymine!

Back 58

Uracil

Front 59

_______(1) bases on RNA paired with bases on DNA.

Back 59

1.) Nitrogenous

Front 60

When Nitrogenous bases of RNA are paired with bases of DNA, it produces four new Complimentary Pairs. Name them.

Back 60

Adenine - Thymine
Cytosine - Guanine
Guanine - Cytosine
Uracil - Adenine

Front 61

What are the three Functional types of RNA.

Back 61

mRNA – Messenger RNA
rRNA – Ribosomal RNA
tRNA – Transfer RNA

Front 62

(ATP – Adenosine Triphosphate)
Provides ______(1) for cell to carry out its function
Formed by breakdown of ______(2).

Back 62

1.) Energy
2.) Glucose

Front 63

Do we store ATP (Adenosine Triphosphate)?

Back 63

No, we make it and then immediately use it.

Front 64

Whatever you _______ is how much your body makes of ATP each day.

Back 64

Weight

Front 65

(ATP - structure)
When high energy bonds are _____ the energy
in the bond is released for cellular use.

Back 65

Hydrolyzed

Front 66

(ATP Breakdown)
ADP = ________ __________(1).
Inorganic ______(2) group [Pi].
and ________(3).

Back 66

1.) Adenosine Diphosphate
2.) Phosphate
3.) Energy

Front 67

(ATP Breakdown)
The reaction is reversible when enough energy is available to re-attach 3rd _______ group.

Back 67

Phosphate

Front 68

(ATP Production)
ATP consumed within _________ (time length).
Continuously replenished.

Back 68

60 Seconds

Front 69

Without ATP , _____(1) can’t do work and life ______ (2) stop.

Back 69

1.) Cells
2.) Processes

Front 70

(Other Nucleotides)
GTP = _________ __________(1).
GTP is involved in ________ ______(2).

Back 70

1.) Guanosine Triphosphate
2.) Energy Transfer

Front 71

(Other Nucleotides)
cAMP = _______ _________ _________ (3)

Back 71

Cyclic Adenosine Monophosphate

Front 72

(Nucleotide- Cyclic Adenosine Monophosphate)
Second messenger – important in ______(1) function.
Formed by removal of both high energy Pi’s from ___(2).
Becomes “second messenger” within ___(3) and activates effects inside it.

Back 72

1.) Hormone
2.) ATP
3.) Cell

Front 73

The study of cells is _______(1).
The ____(2) prefix refers to this as well.

Back 73

1.) Cytology
2.) Cyt

Front 74

(Other Prefixes:)
Inter - means ______(1).
Intra - means ______(2).
Endo - means ______(3).
Extra - means ______(4).

Back 74

1.) between
2.) within
3.) within
4.) outside

Front 75

The cell is basic _______(1) & ______(2) unit of the body.

Back 75

1.) structural
2.) functional

Front 76

The cell is an _________ unit, able to carry on all functions necessary to stay alive & to reproduce itself.

Back 76

Independent

Front 77

The cell chemically primarily consists of these 5 elements.

Back 77

Carbon
Hydrogen
Oxygen
Nitrogen
Trace amounts of other elements

Front 78

The cell comes in all shape and sizes, their are over 200 kinds. They are usually highly ______(1), and are large to extend from ______ to ______ (2)

Back 78

1.) Specialized
2.) Spinal Cord to feet

Front 79

Name the three major parts of the cell.

Back 79

Plasma Membrane
Nucleus
Cytoplasm

Front 80

(Plasma or Cell Membrane)
Boundary to maintain cell’s integrity
Controls which materials get in & out of the cell (this is called _______(1).
Communicates with other cells via specialized _____(2) on its surface.

Back 80

1.) Selective Permeability
2.) Proteins

Front 81

The theory describing structure of Plasma or Cell Membrane is ______ ________ _______(1).
It has a double Layer of ________(2),
and ______(3) embedded in a mosaic pattern.

Back 81

1.) Fluid Mosaic Model
2.) Phospholipids
3.) Proteins

Front 82

(Plasma or Cell Membrane)
__________(1) = water soluble.
Form outer surfaces of ______(2).
__________(2) =water insoluble.
fatty acid part tails.
Face _________(4).
Prevent water soluble materials from passing through membrane

Back 82

1.) Hydrophilic
2.) Membrane
3.) Hydrophobic
4.) interior

Front 83

(Plasma or Cell Membrane)
In the Fluid Mosaic Model, their are _____(1) molecules embedded in bilayer that stabilize ____(2). They also make less ____(3) to water soluble molecules.

Back 83

1.) Cholesterol
2.) Membrane
3.) Permeable

Front 84

(Plasma or Cell Membrane-Glycolipids)
Have short CHO chains.
______(1) bonded.
Only on extra cellular face of ______ ______(2).
Contribute to glycocalyx.

Back 84

1.) Covalently
2.) Plasma Membrane

Front 85

The two distinct types of proteins in membrane are ____ ____(1) and ____ ___(2)

Back 85

1.) Integral proteins
2.) Peripheral proteins

Front 86

(Proteins in Cell Membrane)
Integral proteins
Many are ______(1) (small CHO groups attached).
Most Pass completely through the bi layer.
Have surfaces on both sides of membrane called ______ ______ (2).
Globular (Functional).
Transportation systems-Important in _______(3) and ______(3).

Back 86

1.) Glycoproteins
2.) Transmembrane proteins
3.) nerve signal and muscle contraction

Front 87

(Integral proteins : Gated Channels)
________(1) - voltage changes across PM
Chemical or ligand regulated (ligand: specific chemical-binds to receptor site on protein)
Triggers gate.
_________(2) : physical stress

Back 87

1.) Electrical
2.) Mechanical

Front 88

(Integral proteins : Gated Channels)
Channel Proteins
Act as a carrier - bind to a substance to move it through the _____ ______(1).
Some serve as recognition sites or _______(2).
Identify & attach to _____(3) important to cell function.

Back 88

1.) Plasma Membrane
2.) Receptors
3.) Molecules