Protein

Complex chain of molecules made of amino acids—contain C, H, N, O

Transport, structure, enzymes, hormones, antibodies, fluid balance, pH, channels and pumps

Carboxyl group, amino group, hydrogen and a side chain or R group

Be able to calculate .8grams per kilogram body weight

C, H, N, O

Must be consumed in the diet-body can not make

Can be made by the body

20

9

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Give food examples. Contains all of the essential AA All animal proteins and soybeans

And give food examples Does not contain all of the essential AA All plant based protein sources: legumes, grains, nuts/seeds and vegetables

The amino acid in an incomplete protein that is in inadequate amounts. Legumes are limited in methionine an cysteine Grains are limited in lysine Vegetables are limited in lysine methionine and cysteine

•Combining two incomplete protein sources that provide the limiting amino acids in the other thereby making a complete protein. • Grains, nuts and seeds are high in Methionine and cysteine so consuming one of these with legumes would complement the protein. • Legumes are high in lysine so grains need to be complemented with grains • Vegetables need to be complemented with legumes and grains, nuts or seeds Ex. Beans and rice. Peanut butter and crackers,

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R group, defines which AA it is

Bond between AA (between carboxyl and amino group)

2 AA jointed by peptide bond 3 AA 4+ AA

Strands of aa-joined by peptide bond

Chemical attractions between the side groups of AA-results in bending/folding of the strand What is meant by the term "tertiary stru

>1 AA strand interacting. Establishes chemical bond between 2 or more strands to form a larger protein

Breaking the chemical attraction btwn strands and w/in the strand.

Breaks the electrical charges the chains straighten out. Lose their 3D shape and interactions to other strands of A.

Heat, enzymes, acid and force (ie whipping)

Connective tissue made from protein

Defensive proteins that the body manufactures to destroy foreign invaders. (viruses, bacteria, allergens)

Inside of the blood vessels

Outside the blood vessels

Low pH-excess H ions in the blood

High pH-too few H ions in the blood

Accepts or donates H ions maintaining pH in the blood

N from amine group is converted to ammonia when an amino acid is broken down for energy. If ammonia levels get too high in the blood it becomes more acidic. The body eliminates excess ammonia via the urea in the urine.

Ammonia is converted to urea—a by product of protein metabolism that can be excreted in the urine Define nitrogen balance Amt of N consumed compared to amount of N excreted in the form of urea. Used to help determine if protein needs are being met. What is the name of the inactive form of pepsin and how is it activated? Pepsinogen. Stomach acid activates it Define protein turnover: Constant synthesis and breakdown of proteins in the body. In active form of the enzyme (trypsinogen, chymotripsinogen, carbopeptidase) What is trypsin and where is it manufactured and where does it digest protein? Enzyme—breaks amino acid chains into smaller pepide chains of di and tripeptides and polypeptides-manufactured in the pancreas and secreted into the duodenum of the small intestine

The individual consumes more nitrogen (protein) then is excreted. This means that the body is retaining or adding protein. This is seen during times of growth, pregnancy, recover from illness or in protein deficiency

Excretes more nitrogen then is consumed. Indicates the body is losing protein. Infection, fever, injury, burns, starvation, significant blood loss What is the RDA for protein for adults? .8g/kg

10-35%

Start in stomach, most in s. intestine

Denatures the protein

Breaks down proteins into smaller peptide chains

Stomach

Enzyme—breaks amino acid chains into smaller pepide chains of di and tripeptides and polypeptides-manufactured in the pancreas and secreted into the duodenum of the small intestine

Enzymes—manufactured in the intestinal wall in the brush border where they also break down the dipeptides, tripeptides and polypeptides into free amino acids for absorption. This is the last step of protein digestion

Active and facilitated diffusion

In duodenum and jejunum via active and facilitate transport

The transfer of the amine group from one amino acid to a carbon skeleton to form a different amino acid

Removal of the amino group. Occurs when amino acids are broken down for energy

DNA is read by mRNA in the nucleus of the cell mRNA takes code to the ribosome where tRna reads the code and "fetches" the correct amino acid from the amino acid pool. The amino acid is bonded to adjacent amino acids to form a peptide bond. Once all the amino acids are attached the primary structure of the protein is complete.

DNA determines the type and placement of AA in the protein strand. The type of protein that is manufactured is determined by the genetic code of the DNA which tells RNA which AA to place where. If a particular AA can not be found then the protein cannot be made.

Protein synthesis stops

The amino group is removed and the nitrogen is incorporated into urea which is then eliminated in the urine

Free AA found in the general circulation, cells, tissues and liver--from breakdown of cells and protein consumption. Used to build proteins, make nonessential AA, and for energy.

Breaking down of protein containing compounds in the body to AA where the AA can be recycled into new proteins

B12, Vitamin D, Riboflavin, Iron, Calcium and zinc

There is some research indicating that high intakes of protein increase may effect the following: Kidney function , increased calcium losses leading to osteoporosis, obesity, heart disease, cancer, gout

A type of protein energy malnutrition characterized by significant protein inadequacy with moderate energy deficiency. Symptoms: edema, muscle wasting, increased infection

A Type of protein energy malnutrition characterized by severe inadequate intake of both calories and protein. Symptoms: NO edema, severe loss of muscle, fat and other body tissue