Ch. 3 Protein Structure And Function

Front 1

chemical evolution

Back 1

Chemical reactions in the atmosphere and ocean of ancient Earth are thought to have led to
the formation of the first complex carbon-containing compounds.

Front 2

H2, N2, NH3, and CO2. (organic compounds)

Back 2

Foundation for amino acid

Front 3

Organic compounds reacted to form:

Back 3

mid-sized molecules, such as amino acids, nucleotides, and sugars.

Front 4

Mid-sized, building-block molecules linked to form:

Back 4

proteins, nucleic acids, and complex carbohydrates.

Front 5

proteins, nucleic acids, and complex carbohydrates chemical subunits joined together:

Back 5

Proteins are composed of amino acids, nucleic
acids are composed of nucleotides, and complex carbohydrates
are composed of sugars.

Front 6

Life became possible when:

Back 6

A complex molecules acquired the ability to replicate itself.

Front 7

Enyzmes

Back 7

Are Catalyzed Proteins that speed up chemical reations

Front 8

Building blocks of proteins:

Back 8

Amino acids

Front 9

All Amino Acids Have the Same General Structure.

Back 9

1. H—a hydrogen atom
2. NH2—an amino functional group
3. COOH—a carboxyl functional group
4. a distinctive “R-group” (often referred to as a “side chain”)

Front 10

Protiens are made up of

Back 10

20- amino acids

Front 11

Properties of amino acid varies because:

Back 11

Each of the 20 R-groups is unique

Front 12

Another name for R-group

Back 12

The R-groups, or side chains

Front 13

R-group (side-chains) distinguish amino acids into four general types

Back 13

Acidic
Basic
Uncharged polar
Nonpolar

(It varies due to whatever amino acid in question)

Front 14

How Do Amino Acids Link to Form Proteins?

Back 14

amino acid, a nucleotide,
or a sugar is called

Front 15

Amino acid, a nucleotide, or a sugar is called

Back 15

Monomer (“one-part”).

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Polymer (“many-parts”).

Back 16

A large number of monomers are bonded together

Front 17

The process of linking monomers together is called

Back 17

Polymerization

Front 18

Amino acid monomers can polymerize to
form

Back 18

proteins.

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Macromolecule

Back 19

a very large molecule that is made up of smaller molecules joined together.

Front 20

Proteins Are:

Back 20

Macromolecules—polymers—that consist of
linked amino acid monomers.

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Polymerization = Synthesis

Back 21

iequires energy and is nonspontaneous

Front 22

Monomers polymerize through:

Back 22

condensation (dehydration) reactions

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Hydrolysis (Decomposition)

Back 23

That breaks polymers apart by adding a water molecule

Front 24

Covelant (Peptide Bonds)

Back 24

Bond the carboxyl group of one amino acid
to the amino group of another

Front 25

Polypeptide

Back 25

A chain of amino acids linked by peptide bonds ( which forms nails, hemoglobin blood)

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Polypeptides Proteins

Back 26

Polypeptides containing more than 50 amino acids

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Oligopeptides (peptides)

Back 27

Polypeptides containing fewer than 50 amino acids

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What Do Proteins Do?

Back 28

Catalysis, Defense, Movement, Signaling, Structure Transport

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Catalysis

Back 29

A substance that speeds up chemical reaction without itself being changed.

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Active Site

Back 30

Location in enzyme where substrates are captured( which is ready for a reaction)

Front 31

How many structures (which is the unique sequence of amino acids) does protein have?

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(4. of them)

1 Primary
2 Secondary
3 Tertiary
4 Quaternary

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Primary (Protein Structure)

Back 32

The sequence of amino acids in a polypeptide

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Secondary (Protein Structure)

Back 33

Formation of α-helices and
β-pleated sheets in a polypeptide

Front 34

Tertiary (Protein Structure)

Back 34

Overall three-dimensional shape
of a polypeptide (includes
contribution from secondary
structures)

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Quaternary (Protein Structure)

Back 35

Shape produced by combinations
of polypeptides (thus, combinations
of tertiary structures)

Front 36

Substrates

Back 36

Captured by the enzyme active opening, to either break apart or form products. ex. The break down of bread forms gluclose and break that down to form energy.

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Enyzmes are very specific

Back 37

Each enzyme can only bond to 1 type of substrates.

Front 38

Enzyme Catalysis

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1. Initiation (substrated enter)
2. Transition state facilitation (Interactions between the substrate and active site)
3. Termination (Reaction products are released from the enzyme) *Enzyme is unharmed & recycled*

Front 39

What effect enzymes

Back 39

Certains temperatures and Ph balance

Front 40

How to turn on enzymes

Back 40

1.Cofactors (small inorganice, not made up from carbon) example: hemoglobin

2.Coenzymes (organic) Vitamin B1

Front 41

Stopping enzymes reactions

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1. Competitive inhibition (a molecule similar in size and shape sits in the active site instead of the substrate)***Hince the name Compete it's competing***

2. Allosteric regulation (Different shape covers up active site) (OR) it can make it form another shape.

Front 42

Phosphorylation

Back 42

turns many protein enzymes on and off, thereby altering their function and activity

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Metabolic Pathway

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o A series of reactions

o Each catalyzed by a different enzyme

o To build biological molecules

Front 44

Feedback inhibition occurs when;

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An enzyme in a pathway is inhibited
By the product of that pathway

Pathway can shut down when
Products are no longer needed by the cell

Front 45

Retro-evolution

Back 45

Repetition of backward process
Produces multistep metabolic pathway