Nutrition Chapter 4 Protien

Front 1

What are proteins?

Back 1

-Proteins are large complex molecules
-play many critical roles in the body,
-made of amino acids
-They do most of the work in cells and are required for the structure, function, and regulation of the body’s tissues and organs.

Front 2

How are they unique from carbohydrates and fats?

Back 2

contains nitrogen atoms.

Front 3

structure and characteristics of amino acids

Back 3

1) amino group,
2) acid group
3) hydrogen atom
4) side group,
5) all attached to a cabon atom.

Front 4

How many amino acids are there? Essential? Nonessential?

Back 4

-20 amino acids
-body cant make essential: 9
- nonessential:12

Front 5

protein digestion

Back 5

-Protein Digestion In The Stomachbegins in the stomach, where hydrochloric acid, secreted in the stomach's gastric acid, attacks the protein molecules separating them and breaking them down into amino acids. Then the gastric enzyme pepsin - the only protease able to digest collagen (the fibrous protein found in animal connective tissue) - starts to digest the amino acids.
-Protein Digestion In The Small Intestine,Digestion of proteins continues in the duodenum, the first segment of the small intestine. As in fat digestion, the pancreas helps the process by secreting the pancreatic protease enzymes trypsin and chymotrypsin. Like pepsin, trypsin breaks down a protein into single amino acid molecules, through a process called hydrolysis. During hydrolysis, a water molecule is inserted between the two amino acids which are bonded together. This breaks the bond between them. After breakdown, the amino acids are small enough to pass through the intestinal lining into tiny veins (capillaries) in the villi (the finger-like projections on the wall of the small intestine). Once in the bloodstream, the amino acids are distributed by both red blood cells and by the liquid blood plasma to tissues throughout the body where they are used in the creation and repair of cell structures. Such is the demand for protein, the body maintains a constant balance of amino acids in the blood.

Front 6

What is denaturation?

Back 6

- When protiens are subject to hard conditions.
-They uncoil, loose there shapes, and loose there ability to function.

Front 7

protein synthesis:

Back 7

1) transcription
2) Initiation
3) Elongation
4) Termination

Front 8

transcription

Back 8

1. Transcription
Before Protien synthesis, the corresponding RNA molecule is produced by RNA transcription. One strand of the DNA double helix is used as a template by the RNA polymerase to synthesize a messenger RNA (mRNA).

Front 9

translation

Back 9

Translation
The ribosome binds to the mRNA at the start codon (AUG) that is recognized only by the initiator tRNA. The ribosome proceeds to the elongation phase of protein synthesis. During this stage, complexes, composed of an amino acid linked to tRNA, sequentially bind to the appropriate codon in mRNA by forming complementary base pairs with the tRNA anticodon. The ribosome moves from codon to codon along the mRNA. Amino acids are added one by one, translated into polypeptidic sequences dictated by DNA and represented by mRNA. At the end, a release factor binds to the stop codon, terminating translation and releasing the complete polypeptide from the ribosome.

Front 10

amino acid sequence?

Back 10

G-G-G-G

Front 11

roles of protein in the body?

Back 11

1) Antibodies defend the body from germs.
2) Contractile proteins are responsible for movement.
3) Enzymes speed up chemical reactions.
4) Storage proteins store amino acids.

Front 12

• What happens if you eat too much protein?

Back 12

-leeching of calcium from the bones
- Kidney Malfunction

Front 13

• What foods are considered high quality proteins?

Back 13

eggs, milk, fish, cheese,

Front 14

complementary proteins?

Back 14

Any protein that is incomplete on its own but may become complete when combined with other proteins to provide all of the amino acids necessary for normal metabolism.

Front 15

limiting amino acid?

Back 15

- 3 amino acids that are a little harder to get than the rest, thus it is important to make sure you’re getting enough of these three.

-limiting amino acids, because if a person’s diet is deficient in one of them, this will limit the usefulness of the others,even if those others are present in otherwise large enough quantities.

- The amino acids sulfur-containing ones (methionine and cysteine), tryptophan, and lysine.

Front 16

RDA
for protein for healthy adults

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-0.6 grams per kilogram of body weight;

-RDA is 0.8 grams this is said to meet 97.5% of the population's needs.

Front 17

• What is deamination?

Back 17

- amino group of a protein is being separated from the acidic group.

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Polypeptide

Back 18

-10 or more Amino acids bonded together

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Tripeptide

Back 19

- 3 amino acids bonded together

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dipeptide

Back 20

- 2 amino acids bonded together

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peptide bond

Back 21

- bond that connects acid end and amino end of another protien chain

Front 22

non essential amino acids

Back 22

the body makes them

Front 23

proteases

Back 23

enzymes that hydrolize protien

Front 24

pepsin

Back 24

a gastric enzyme that hydrolizes protien

Front 25

hemoglobin

Back 25

large globular protien moleule that that packs red blood cells

Front 26

Protien synthesis

Back 26

1) Delivers instuctions
2)Lining up amino acids
3) Sequencing errors
4) Ntrients Gene Expression

Front 27

translation

Back 27

Messenger Rna directing sequence of amino acids and synthesis of protiens

Front 28

transcription

Back 28

Messenger RNA being made from a template of Dna

Front 29

proteomics

Back 29

Study Of Body's protien