Reading...
Play button
Play button
Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
23 Cards in this Set
- Front
- Back
|
Protein
Size |
Number of amino acids in the primary sequence determines the size
Oligopeptide - 3-10 amino acids 100 amino acids is a protein Proteins cn be even up to 2000 amino acids in length Oligopeptides are too small to form a true tertiary or quarternary structure, although they can fold a little |
|
|
Protein
Function |
The shape of a protein determines its function
Proteins pushed outside of their optimal temperature and pH denature and stop functioning |
|
|
Proteins
Types |
Fibrous
|
|
|
Fibrous Proteins
|
Structural proteins
They are insoluble fibers Don not have a tertiary structure Usually trihelical structures held together by disulfide covalent bonds - 3 strands braided together Ex: keratin - found in hair and nails, and the outside of the epidermis |
|
|
Fibrous Proteins
Keratin |
The protein conformation is an alpha helix
Alpha helix looks like a coiled telephone cord Each amino acid in the cord is related to the next by a 1.5 angstrom rise in the alpha helix |
|
|
Fibrous Proteins
|
A second type of protein conformation found in the silk protein fibroin and strands of a spider's web is the beta cornformation called a Beta pleated sheet
|
|
|
Fibrous Protein
Collagen |
Collagen displays a helical conformation, but not an alpha helix
Collagen's basic unit is tropocollagen which is 3 braided strands - 2 are similar and one is different |
|
|
Types of Collagen
|
Type I
Type II Type III Type IV |
|
|
Type I Collagen
|
Most common
Found in skin, tendon, bone, and cornea of the eye |
|
|
Type II Collagen
|
Found in fibrocartilage such as the menisci (knee) and intervertebral disks
|
|
|
Type III Collagen
|
Found in fetal cardiovascular tissue
|
|
|
Type IV Collagen
|
Component of basement membrane which helsps to anchor simple epithelial cells
|
|
|
Protein Structure
Globular Proteins |
Have tertiary and quarternary conformation
They are soluble, spheroid, compact structures Ex: Enzymes, antibodies, hemoglobin, myoglobin |
|
|
Enzymes
|
Enzymes are biological catalysts
They lower the activation energy required for a reaction They increase the rate of reaction Highly specific - 1 enzyme exists for each chemical reaction in the body They are affected by pH and temperature - have optimum ranges |
|
|
Enzymes
|
Composed of a protein portion and a non-protein portion
Protein part is called the apoenzyme Non protein part is called the coenzyme The apoenzyme and coenzyme represent the holoenzyme which is the functional enyme entity Coenzymes are organic; if it is inorganic (like a metal), it is called a cofactor |
|
|
Enzyme Reactions
|
Reactants (substrate) bind to the active site of the enzyme and interact to yield the product
Cofactors and coenzymes must bond to the enzyme before the substrate Coenzymes are commonly from vitamins see pic pg. 10 and 11 |
|
|
Nucleic Acids
|
DNA and RNA
Store and process information at the molecular level Made up of purines and pyrimidines DNA is a double stranded helix - makes up chromosomes and genes |
|
|
Purines
|
Adenosine
Guanine |
|
|
Pyrimidines
|
Cytosine
Thymine (only in DNA) Uracil (only in RNA) |
|
|
Nucliec Acids
|
Nucleic acids are chains of nucleotides
A nucleotide consists of a sugar, a phosphate, and a nitrogenous base |
|
|
Nucleotides
|
Building blocks of nucleic acids
Sugar: deoxyribose (DNA) or ribose (RNA)deoxyribose lacks oxygen DNA bases - adenine, thymine, cytosine, guanine RNA bases - adenine, uracil, cytosine, guanine |
|
|
ATP
|
Adenosine triphosphate
High energy compounds Cellular energy is stored in high energy bonds Adenosine diphosphate (ADP) becomes ATP through phosporylation |
|
|
ATP
|
Adenine bonds with ribose and phosphates
see pic pg. 14 |
