Term
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Definition
| 50% in animal-based and 50% in plant-based |
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Term
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Definition
2 levels: Protein is digested into AA that are used to synthesize proteins in the body.
Protein in food
(digested)
Amino Acids
(protein synthesis)
Protein in the body |
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Term
| Proteins, out of all the macromolecules is the: |
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Definition
| most diverse in terms of function. THey are the workers- whatever the job is, the proteins get it done |
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Term
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Definition
Finish this NC pg 129
regulatory-
structural-
Energy- |
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Term
| what are the structures of proteins? Altering the structure? |
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Definition
Structure for proteins is everything- altering it alters the functions
primary
secondary
tertiary
quaternary |
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Term
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Definition
| molecules made up of one or more chains of amino acisd. Some contain few, some contain thousands |
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Term
| How many aa? What is the common structure? |
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Definition
| 20 and each consists of an amine group, central carbon, and an acid group and a side chain (functional group) |
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Term
Charges:
amine group
acid group |
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Definition
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Term
| What makes one AA different from the next? |
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Definition
| off the central carbon there is a functional group/Side "R" chain that is unique from each AA. |
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Term
| how can side chains be different from each other? |
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Definition
Different in:
Charge
Size
Hydrophilic/hydrophobic
essential/nonessential (9 essential/11 non) |
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Term
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Definition
| our body can't make that side chain (9 of them) |
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Term
| What are the bonds that hold AA together? |
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Definition
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Term
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Definition
| condensation reaction: produces water. |
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Term
| How are proteins classified? |
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Definition
| Based on number of amino acids |
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Term
Dipeptide
tripeptide
polypeptide
What are most proteins? |
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Definition
2 AA
3 AA
Over 20 AA
Mst are polypeptides |
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Term
| Protein Structure levels: |
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Definition
Amino Acid
Polypeptide- chain of AA attached by peptide bonds
Protein- specific sequence and number of aa
Primary, Secondary, Tertiary, Quaternary structure |
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Term
| What is the primary structure of proteins? Determined by? |
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Definition
The number and sequence of AA in a protein. Each protein class has its own unique primary structure
Determined from a genetic code in DNA from nucleus of each cell. |
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Term
| What is the Secondary structure of proteins? |
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Definition
| Amine groups and carboxylic acid groups have positive and negative charges respectivily. These attract and repel each other. Cases the protein to fold in organized and predictable patterns. This folding is called the secondary structure of a proteins. These attractions are held together by hydrogen bonds. |
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Term
| What are the two most common folding patterns of secondary proteins ? |
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Definition
alpha-helix
beta- folded sheet |
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Term
| What is the tertiary structure of proteins? |
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Definition
| Additional folding of the protein is due to interactions between the R groups of AA and between amino acids and the surrounding environment. This level of folding gives the rise to the 3-D configuration |
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Term
| Primary+secondary+tertiary give proteins: |
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Definition
| A 3D configuration, refered to protein conformation |
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Term
| What is the quaternary structure of proteins? Which proteins have it? Example? |
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Definition
consists of several polypeptide chains coming together to form the final protein.
Only proteins made from polypeptide chain can have a quaternary structure
Hemoglobin 4 polypeptide chains |
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Term
When the protein structure is disrupted (not the peptide bonds) what happens?
Denaturation-
Genetic abnormality- |
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Definition
the functionality of the protein is lost bc structure= function
Denaturation- disrupts the weak ionic attractions and hydrogen bonds that hold the secondary and tertiary structure
Genetic abnormality- alterations in the primary structure. |
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Term
Proteins are -
Shape can be altered by- |
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Definition
fragile
denaturing agents such as: heat, acid, heavy metals, UV light |
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Term
| What do denaturing agents do? What happens once a protein is denatured? |
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Definition
disrupt the weak hydrogen bonds and ionic bonds, causing the protein to unfold.
Once a protein has been denatured (altered shape) they lose there functional capacity. They retain their primary structure and nutritional value |
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Term
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Definition
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Term
| Inherited Genetic disorders and protein: |
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Definition
| DNA in cell directs protein synthesis. IF DNA has an error (mutation) the primary structure (seq. of AA) is altered. This changes the shape of the protein and thus its biological activity. |
|
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Term
| what is sickle cell disease? |
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Definition
an inherited condition characterized by sickle-shape red blood cells and hemolytic anemia
The RBC contain an abnormal dorm of hemoglobin, the protein that carries oxygen. The altered shape occrs bc valine replaces glutamic acid in the AA sequence of one of the hemoglobins polypeptide chain. As a result of one alteration the hemoglobin has diminished ability to carry oxygen |
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Term
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Definition
By specific protein-splitting enzymes known collectively as proteases (hydrolyze peptide bonds)
Source of protease enzymes:
stomach, pancreas,and the small intestine is a source of activating enzymes not protease |
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Term
| How are many proteases secreted? |
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Definition
| AS proenzymes which are inactive enzyme precursors. When proenzymes are released they are activated by other enzymes or surrounding conditions |
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Term
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Definition
| stimulates the release of the hormone gastrin. Gastrin stimulates the release of gastric juice (HCL, water, enzyme- pepsinogen-inactive form of enzyme). HCL dentatures the protein facilitates enzymatic digestion by exposing peptide bonds, converts inactive pepsinogen into active form pepsin. Pepsin hydrolyzes specific peptide bonds into shorter polypeptide chains which move into the small intestine. |
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Term
| When polypeptides enter the small intestine: |
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Definition
| it stimulates the release of the hormones CCK from the lining of the small intestine, which stimulates the relase of pancreatic juice- proteolytic enzymes released from the pancreas are in an inactive (proenzyme) form. Includes Trypsinogen, Chymotripsinogen, Procarboypeptidase |
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Term
| explain the activation of pancreatic proteolytic enzymes in the small intestine |
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Definition
enterokinase activates trypsinogen into the active form of trypsin
Trypsin activates chymotrypsinogen and procarboxypeptidase into the active enzyes of chymotrypsin and procarboxypeptidase |
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Term
| What do the trypsin, chymotrypsin and caboxypeptidase and intestinal proteases do? |
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Definition
| hydrolyze remaining peptide bonds. |
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