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UF / Science / HUN 2201 / How to describe proteins differ from carbohydrates and lipids?

How to describe proteins differ from carbohydrates and lipids?

How to describe proteins differ from carbohydrates and lipids?

Description

School: University of Florida
Department: Science
Course: Fundamentals of Human Nutrition
Professor: Laura acosta
Term: Fall 2018
Tags: Lipids and Proteins
Cost: 50
Name: HUN2201 Exam 2 Study Guide
Description: Content on this study guide will be presented on the exam
Uploaded: 10/01/2018
10 Pages 6 Views 14 Unlocks
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Exam 2 Study Guide


How to describe proteins differ from carbohydrates and lipids?



Proteins:

1. Describe how proteins differ from carbohydrates  and lipids.

∙ Differ because of their chemical composition ∙ Presence of Nitrogen makes them unique

2. Identify the structure of an amino acid molecule  including its five essential components.

∙ Chain of amino acids contained by a peptide bond  with a side chain

∙ Contains a central carbon atom, also known as the  alpha (α) carbon, bonded to an amino group (NH2),  a carboxyl group (COOH), and to a hydrogen atom.


How to identify the structure of an amino acid molecule and its five essential components?



5 Essential Components: 

1.A central carbon atom  

2. A hydrogen atom  

3. An amino group - consisting of a nitrogen atom  and two hydrogen atoms  

4. A carboxyl group - consisting of a carbon atom, two oxygen atoms, and one hydrogen atom  

5. An R-group or side chain - consisting of varying atoms

3. Differentiate among essential amino acids,  nonessential amino acids, and conditionally  essential amino acids.

∙ Essential amino acid: must be supplied by diet as it CANNOT be made by the body  

***MEMORIZE 9 ESSENTIAL AMINO ACIDS

1. Phenylalanine

2. Valine

3. Threonine

4. Tryptophan

5. Isoleucine

6. Methionine

7. Histidine (only essential for  

infants)

8. Leucine

9. Lysine 

∙ Nonessential Amino Acids: Can be made in  the body (do not need to know the 11 kinds)  


What are the 9 ESSENTIAL AMINO ACIDS?



∙ You don't need to worry about getting  

enough of these amino acids since your body

will compensate for any gaps in your diet

∙ Conditionally Essential Amino Acids: lacks an essential amino acid precursor but can become  essential under certain conditions We also discuss several other topics like khan academy sn1 sn2 e1 e2

∙ 8 out of 11 nonessential AA 

∙ When you’re sick or under significant stress,  your body may not be able to produce  

enough of these amino acids to meet your  

needs.

4. Discuss the factors used to evaluate protein  quality.

∙ Digestibility: If you can’t completely digest and  absorb a protein source, you won’t get the benefits  of all the amino acids the food contains

∙ Essential Amino Acid Composition: highest  quality sources of protein are those that contain all  of the essential amino acids. Such proteins are  called “complete” proteins

5. Explain how proteins are made and the  relationship between protein shape and function.

∙ The synthesis of RNA from DNA is called  

transcription which the mRNAs are then translated into a protein; 1 amino acid is added to the protein  strand for every 3 bases in the RNA

∙ FUNCTION is dependent upon SHAPE

***Once protein structure is denatured, we shift  its function

6. Discuss how proteins are digested and absorbed  by the body.

∙ Before your body can use protein to build and repair tissues, the large molecules of protein must be  digested by enzymes into amino acids. D

1. Digestion of protein begins in your stomach  with the aid of gastric juices. Pepsin from the  

intestinal lining and the pancreas breaks the  We also discuss several other topics like imprinting is a form of behavior that

peptide bonds that hold the protein molecule  

together and digestion continues in the small  

intestine.

2. From there, amino acids are absorbed into the  bloodstream and transported throughout your  body.  

7. Describe deamination, where it occurs in the body, the products produced, and the fate of these  products.

∙ An oxidative reaction that occurs under aerobic  conditions in all tissues but especially the liver

∙ Amino acids are separated as an amino group is  removed if there is an abundance of protein  

admission

1. The breakdown of amino acids releases  

nitrogen-containing amine groups (NH2) which  can be toxic to cells.

2. The liver removes these amine groups via the  process of deamination and converts them into

harmless products keto acid and ammonia  

(which is converted into urea and excreted in  

urine)

8. Explain how the catabolism of proteins differs  from the catabolism of carbohydrates and lipids.

∙ Carbohydrates, fats, and proteins are broken down  into their individual monomer units: carbohydrates  into simple sugars, fats into fatty acids and glycerol, and proteins into amino acids

1. After deamination, the carbon skeletons of amino  acids can be oxidized for energy.  

2. The carbon skeletons of glucogenic amino acids are  converted into pyruvate, whereas those of  

ketogenic amino acids are converted into acetyl  CoA

3. The end products of protein catabolism are carbon  dioxide, water, ATP, and urea (which lipids and  carbohydrates don’t produce)

9. Explain nitrogen balance We also discuss several other topics like reli 180 unc

∙ measure of nitrogen input minus nitrogen output ***Nitrogen Balance = Nitrogen intake - Nitrogen loss.

∙ Sources of nitrogen intake include meat, dairy, eggs,  nuts and legumes, and grains and cereals

∙ Examples of nitrogen losses include urine, feces, sweat,  hair, and skin.

10. Describe at least four functions of proteins in the  body.

1. Anabolism: Source of nitrogen & EAA

2. Structural and Mechanical Functions

3. Transport: Carriers and membrane pumps

4. Enzymes: Catalyze metabolic reactions

5. Hormones: Regulate body processes

6. Immunity: Antibodies are proteins

7. Fluid Balance: Vascular proteins attract water 8. Acid-Base Balance: Buffer

∙ Source of Glucose

∙ Source of Energy: 4 kcals

11. Calculate your Recommended Dietary Allowance  for protein.

To estimate RDA Protein intake:

1. Take weight in lbs (ex. 150) and divide by 2.2 to  convert to kg (ex. 150/2.2=68.2 kg)

2. Multiple kg weight (68.2kg) by 0.8g to get grams of  protein recommendation

3. (ex. 68.2kg x 0.8g = 54.56g protein/day)

12. Identify the potential health risks associated with  high-protein diets.

∙ Some high-protein diets include foods such as red  meat and full-fat dairy products, which may  If you want to learn more check out pip calcium signal mechanism

increase your risk of heart disease and contribute to high cholesterol

∙ A high-protein diet may worsen kidney function in  people with kidney disease because your body may  have trouble eliminating all the waste products of  protein metabolism

13. List six foods that are good sources of protein,  including at least three non-meat sources.

1. Egg

2. Tofu

3. Meat/ Poultry

4. Greek Yogurt

5. Potatoes

6. Quinoa

14. Describe two disorders related to inadequate  protein intake or genetic abnormalities.

1. Kwashiorkor: protein efficiency

∙ Immune system and hormones are impaired  ∙ Low blood albumin

∙ Edema (tissue swelling): water is leaking into  stomach and cause inflation

2. Marasmus: general starvation

∙ Muscle and fat wasting If you want to learn more check out amt 595 class notes
Don't forget about the age old question of thomas douglas uci

∙ Slowed metabolism

∙ Impaired brain development

15. Define the types of vegetarian diet, health risks  and health benefits

1.Lacto Vegetarian: Lacto-vegetarians do not  eat red or white meat, fish, fowl or eggs.  

However, lacto-vegetarians do consume dairy  

products such as cheese, milk and yogurt.

2. Ovo Vegetarian: Ovo-vegetarians do not eat  red or white meat, fish, fowl or dairy products.  However, ovo-vegetarians do consume egg  

products.

3. Lacto-ovo vegetarian: Lacto-ovo vegetarians do not consume red meat, white meat, fish or  

fowl. However, lacto-ovo vegetarians do  

consume dairy products and egg products. This is the most common type of vegetarian.

Benefits: May reduce heart disease, cancer, and type 2  diabetes

Risks: Lack of protein, Vitamin B, Iron, and Omeg-3  Fatty Acid intake

Lipids

1. Describe the types and  structure of lipids in the diet.

 1.Saturated Fatty Acid: 

1. Structure is straight

2. Saturated with hydrogen

3. ONLY Single Bonds NO double bonds

 2.Monounsaturated Fatty Acid: 

1. Double bond allows susceptibility for oxidation 2. Loose hydrogen  

3. MUFA (olive oil has a lot)

 3.Polyunsaturated Fatty Acid:  

1. 3 double bonds

2. PUFA  

2. Understand how structure  of lipids dictate digestibility and function.

∙ Those with longer fatty acid associated with it  (triglyceride) are stacked and become more easily  solid  

∙ High in saturated fats may liquidly if the length of  the fatty acid is shorter  

∙ Shorter fatty acid chains (like in coconut oil) can  move around more and thus melt

3. List the functions of  specific lipids in the body.

1.Triglyceride functions:

∙ Taste/Texture

∙ Storage form of energy

∙ Supply essential fatty acids

∙ Carrier of fat-soluble compounds

2.Phospholipids:

∙ Part of cell membrane and lipoprotein  

compound

∙ Emulsifier in foods (keeps water and fat  

mixed)

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