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Ch. 22 Proteins

Structure Proteins Collagen and keratin make up skin, bone, hair, nails
Catalysts Proteins All reactions in living systems are catalyzed by enzymes
Movement Proteins Muscles are made up of myosin & actin
Transport proteins Hemoglobin transports O2 from the lung cells; other proteins transport molecules across cell membranes
Hormone Proteins Insulin, oxytocin, human growth hormone
Protection Proteins Blood clotting invloves protein fibrinogen; body uses antibodies to flight disease
Storage Proteins Casein in milk and ovalbumin in eggs store nutrients for newborn infants and birds; ferritin in the liver stores iron
Regulation Proteins Certain proteins control gene regulation and control where it takes place
2 structural types of Proteins 1. Fibrous Proteins-long & thin (structural) 2. Globular proteins- everything else (enzymes)
Amino Acid a compd that contains both an amino group and a carboxyl group *in zwitterion form aa are solids with high melting points, water soluble
a-amino acids amino group is on the carbon adjacent to the carboxyl group
Peptides amide bond between the a-carboxyl group of one amino acid and the a-amino group of another
Zwitterion Behavior *at any pH above (basic) its pI, it has a negative charge *Any pH below(acidic) its pI has a positive charge *Proteins are least soluble in water at their isolelectric points and can be precipitated from solution at this pH
# of peptides possible for a chain of n amino acids 20^n
Sickle Cell Anemia a single subsitituion in one amino acid of the b-chain of hemoglobin
a-Helix *all R-groups point outward from helix *C=O group of each peptide bond is H bonded to the N-H group of the peptide bond four amino acid units away from it * the 6 atoms of each peptide bond lie in the same plane
B-Pleated Sheet * R groups alternate from above to below the plane of the sheet *C=O and N-H groups of the peptide bonds from adjacent chains point toward each other are in the same plane so that the hydrogen bonding is possible between them
Tertiary Structure Overall conformation of an entire polypeptide chain
Tertiary Structure is stabilized in 5 different ways 1. Covalent bonds-formation of disfulide bonds between cysteine side chains 2. H Bonds- between polar groups of side chains 3. Salt Bridges- attraction of -NH3+ group and -COO group 4. Hydrophobic Interactions- between nonpolar side chains 5. metalion
Quaternary Structure arrangement of polpeptide chains into a noncovalently bonded to aggregation of protein subunits * the individual chains are held together by h bonds, salt bridges, and hydrophobic interactions
Adult Hemoglobin 2 alpha chains of 141 aa each, and 2 betachains of 146 aa each
Fetal Hemoglobin 2 alpha chains and 2 gemma chains. has a great affinity for oxygen than adult hemoglobin
Myoglobin Storage in muscle; not allosterically
Hemoglobin allosterically regulated protein; transport
Denaturation process of destroying the native conformation of a protein by chemical or physical means; some reversible, some not *agents insclude- Heat: can distrupt H bonding and unfold proteins
Chaperone Proteins heat shock proteins can assist proteins to attain their correct secondary and tertiary structure or facilitate the correct refolding of partially denatured proteins
Which of the following is true of proteins? the acid/base properties of a protein depends on the identity of its side chains
What is true of the isoelectric point amino acids? it is the pH at which amino acid has an equal number of positive and negative charges
Secondary structure is associated with which of the following? h-bonding within the backbone
An example of a structural protein Collagen
How many proteins make up hemoglobin? 4
Having the gene for sickle cell hemoglobin gives an individual enhanced immunity against what disease? Malaria
What type of chemical reaction is involved in the formation of disfulide bonds from thiolds? oxidation
How many atoms from the backbone of the repeat unit of a protein? 6
Why is 70% ethanol rather than 95% ethanol used in sterilizing skin before injections? kills bacteria by penetrating them and coagulating their proteins
When will a protein have the lowest solubility? at is isoelectric point
How many different amino acids are commonly found in proteins? 20
What is true of the atoms in the backbone unit of a protein? they are all in the same plane
What explains the unusually high melting points of amino acids? their existence as zwitterions
Protein synthesis proceeds in what direction? from the N-terminus to the C-terminus
What is the name for proteins which assist other proteins in attaining their correct secondary and tertiary structures? Chaperones
In the tertiary structure of proteins which aa is involved in forming covalent bonds? cysteine
What time of chemical reaction is involved in the conversion of disfulide bonds to thiols? reduction
What determines the characteristics of an aa? the identity of its side chains
Created by: aoyler



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