Proteins

What is a protein?

amino acids

What is the primary function of a protein?

structural or mechanical functions
enzymes
hormones
immune funciton
fluid balance
acid-base balance
transport function
source of energy and glucose

What is the chemical structure of an amino acid?

amino group, one of 20 unique side groups, carboxylic acid group (COOH-)

What are the elements in the chemical structure of the amino acids?

carbon hydrogen oxygen and nitrogen

Define indispensable amino acid (essential amino acids)

amino acids that the body cannot make at all or cannot make enough of to meet physiological needs. must be supplied in the diet

Define dispensable amino acid (nonessential amino acid)

amino acids that the body can make if supplied with adequate nitrogen, do not need to be supplied by diet

How many amino acids are there?

20

How many essential (indispensable) amino acids are there?

9

Define conditional indispensable (essential) amino acids

amino acids that are normally made in the body (dispensable) but become indispensable under certain circumstances, such as during critical illness

What is complete or high quality protein? Give some food examples

proteins that supply all the indispensable amino acids in the proportions the body needs
ex. red meats, poultry, fish, eggs, milk, milk products

What is an incomplete protein or low quality protein? Give some food examples

proteins that lack one or more amino acids
ex. grain products (pasta), legumes

What is a limiting amino acid? Give examples

the amino acid in shortest supply during protein synthesis. also the amino acid in the lowest quantity when evaluating protein quality

What does it mean to complement proteins? Give some food examples

the complementation of a protein is when one protein that is lacking sufficient amino acids is eaten with amino acids that are also insufficient. eating them together makes them complete

What plant source is a complete protein?

soybeans

What is a side group of an amino acid and its role in the type of amino acid?

side group is unique to each amino acid, mean that they differ in shape, size, composition, electrical charge, and pH

What is a peptide bond?

the bond between two amino acids formed when a carboxyl group of one amino acid joins an amino group of another amino acid, releasing water in the process

Define dipeptide, tripeptide, and oligopeptide

dipeptide-two amino acids joined by a peptide bond
tripeptide-3 amino acids joined by a peptide bond
oligopeptide-4-10 amino acids joined by peptide bonds

What is meant by the term "primary structure of an amino acid"?

sequence of amino acids forming one or more polypeptide chains

What is meant by the term "secondary structure of an amino acid?

the coiling or folding of its polypeptide chains due to hydrogen bonding within or between amino acid chains

What is meant by the term "tertiary structure of an amino acid"?

3-dimensional shape of the polypeptide caused by weak interactions among side groups, and between side groups and the fluid environment

What is meant by the term quaternary structure of an amino acid"?

final 3-dimensional structure of a protein formed by all the polypeptide chains

Define denature

an alteration in the three-dimensional structure of a protein resulting in an unfolded polypeptide chain that usually lacks biologoical activity

What happens to the protein when it is denatured?

loses its 3-dimensional shape

Give examples of substances/circumstances that will denature a protein

acidity, alkalinity, heat, alcohol, oxidation, and agitation

Define collagen and the role protein plays

the most abundant fibrous protein in the body, collagen is the major constituent of connective tissue, forms the foundation for bones and teeth, and helps maintain the structure of blood vessels and other tissues

Define antibodies and the role protein plays

large blood proteins produced by B lymphocytes in response to exposure to particular antigens, each antibody specifically binds to to and helps eliminate its matching antigen from the body, once formed, they circulate in the blood and help protect the bod

Define intravascular and the role protein plays

the fluid portion of the blood (plasma) contained in arteries, veins, and capillaries, counts for about 15% of the extracellular fluid

Define extra vascular and the role protein plays

...

Define acidosis and the role protein plays

an abnormally low blood pH due to increased acidity

Define alkalosis and the role protein plays

an abnormally high blood pH due to increased alkalinity

What is a buffer?

compounds or mixtures of compounds that can take up and release hydrogen ions to keep the pH of a solution constant - maintains blood pH

What is ammonia and what is its relationship to protein

...

What is Urea?

a compound made from nitrogenous waste produced in cells

Define nitrogen balance

nitrogen intake minus the sum of all sources of nitrogen excretion; nitrogen balance equals zero

What is positive nitrogen balance and give examples

nitrogen intake exceeds nitrogen excretion, means that the body is adding proteins- children, pregnant women, or people recovering

What is negative nitrogen balance and give examples

nitrogen excretion exceeds nitrogen intake, losing protein , people whoa re starving, in extreme weight loss or who suffer fever, illness, infection

What is the RDA for protein for adults?

.85 grams

What is the AMDR for protein?

10-35%

Where in the digestive tract does the chemical digestion of protein occur?

stomach, small intestine

What is HCL and how does it effect protein digestion?

hydrochloric acid-stimulates pepsinogen- changes into pepsin- denatures and digests proteins

What is pepsin?

Pepsin is an enzyme in the stomach that digests protein and makes amino acids.

Where is pepsin found?

stomach

What is the name of the inactive form of pepsin and how is it activated?

pepsinogen

What is trypsin and where is it manufactured, what is its inactive form and where does it digest protein?

a protease produced by the pancreas that is converted from the inactive proenzyme from (trypsinogen) to the active form (trypsin) in the small intestine

What is chymotrypsin and where is it manufactured, what is its inactive form and where does it digest protein?

a protease produced by the pancreas that is converted from the inactive proenzyme form (chymotrypsin) in the small intestine

What are peptidases and where are they manufactured and what are their roles in digestion?

enzymes that act on small peptide units by breaking peptide bonds

How are amino acids absorbed?

in duodenum and jejunum. transported via portal circulation to liver. then released into general circulation.

Where are amino acids absorbed?

..., lining of the Small intestine

Define transamination

...

Define deamination

The breakdown of excess amino acids in the liver"
Amino acid -> keto acid + ammonia

Describe the steps in protein synthesis

...

What is the relationship between DNA/RNA and protein synthesis

..., the structure of the protein is dictated by the DNA of the gene
Transcription: use of the genetic info in DNA to make mRNA
Translation: conversion of genetic inf mRNA to the amino acids sequence of a protein.

What happens if an amino acid is missing during protein synthesis?

..., ultimately it stops. but if dispensible (nonessential): cell will either make that AA or obtain it from liver. if indispensible (essential): body breaks down its own protein to supply missing AA

What is produced when Amino acids are broken down for energy?

lactic acid

What is the amino acid pool?

the amino acids in the body tissues and fluids that are avaliable for new protein synthesis

Define protein turnover

the constant syn and breakdown of proteins in the body

What are the different types of vegetarians and what do they or don't they eat?

lacto-ovo-vegetarians-milk, cheese, eggs
vegans- no animal based foods
fruitarians-eat only raw fruit, nuts, and green foliage
semi-vegetarian
mediterranean

What nutrients maybe deficient in a vegan diet?

zinc, calcium, vit. D, riboflavin, and vit B12

What are the risks associated with too much protein intake?

kidney function
mineral losses
obesity
heart disease
cancer
gout

What is Kwashiorkor

a type of malnutrition that occurs primarily in young children who have an infectious disease and whose diets supply marginal amounts of every and very little protein.

What is Marasmus

a type of malnutrition resulting from chronic inadequate consumption of protein and energy that is characterized by wasting of muscle, fat, and other body tissues