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CHM 140

CH 22

QuestionAnswer
List the 8 functions of proteins in the body and give an example of each. a)structure (collagen) b)catalysts(enzymes), c)movement(myosin), d)transport(hemoglobin), e)hormones(insulin,GH), f)protection(antibodies), g)storage(casein), h)regulation(of gene expression)
What 3 substances make up the majority of connective tissue? collagen, elastin, proteoglycans
What 5 places in the body is collagen found? tendons, skin fiber, blood vessels, bone, and cartilage
What is the most abundant protein in the body? collagen
Where in the body is elastin found? ligaments
Where are proteoglycans found? extracellular matrix
Where in the body is a-keratins found? hair, nails, and much of the outer layer of skin
What is the purpose of fibrinogen in the blood? blood clotting
What are the two types (shapes) of proteins and what is the structure of each? fibrous (ropelike, linear) and globular (circular, compact)
Where is th amino groups located with respect to the carbonyl carbon? on alpha carbon
A zwitterion is neutral but carries both a ___and ___ charge. + and -
Describe what the isoelectric point (pI) is. pH at which the majority of molecules of a compound in solution have no net charge
What two atoms does a peptide bond bind together. What is the name of this functional group? C and N - amide group
What is the difference between a polypeptide and a protein? # of amino acids: protein has 30 more than a polypeptide
C-terminal amino acid- amino acid at the end of a chain having a free -COO-group
N-terminal amino acid amino acid at the end of a chain having a free -NH3+group
primary structure sequence of amino acids in a polypeptide chain
secondary structure conformations of amino acids in localized regions of a polypeptide chain
tertiary structure overall conformation of a polypeptide chain
quaternary structure arrangement of two or more polypeptide chains into a noncovalently bonded aggregation
What is a glycoprotein? a protein to which one or more carbohydrate units are bonded
What is denaturation? process of destroying the native conformation of a protein by chemical or physical means-can disrupt the secondary, tertiary, or quatenary structure
What are the 3 secondary structures that we studied in class? a-helix, b-pleated sheet, collagen triple helix
An a-helix is most commonly a right or left handed helix? right
How many amino acids per turn in a a-helix? 3.6
Describe the positions of the carbonyl (C=O) groups and the amine hydrogens (N-H) in the a-helix. The amine (N-H) groups point in direction of spiral almost parallel with helix and carbonyl (C=O) groups pointing in opposite direction.
Describe the positions of the R group in the a-helix. The R groups are perpendicular to the axis of the helix
What interaction holds a protein in the a-helical form? hydrogen bonding
Describe the positions of the carbonyl (C=O) groups and the amine hydrogens (N-H) in the b-pleated sheet. The C=O and N-H groups of peptide bonds from adjacent chains point toward each other and are in the same plane so that hydrogen bonding is possible between them
Describe the positions of the R group in the b-pleated sheet. R- groups on any one chain alternate, first above, then below the plane of the sheet, etc.
What interaction holds a protein in the b-pleated sheet form? hydrogen bonding
Describe the structure of collagen. Consists of three helical polypeptide chains wrapped around each other in a ropelike twist to form a triple helix called tropocollagen
What 3 amino acids make up the majority of collagen? Almost 2/3 of collagen is made up of the amino acids: proline, hydroxyproline, and glycine
What 4 interactions hold the protein in its tertiary structure? a)covalent bonds, b)hydrogen bonding, c)salt bridges, d)hydrophobic interactions
What 3 interactions hold the protein in its quaternary structure? a)hydrogen bonding, b)salt bridges, c)hydrophobic interactions
The glycosidic bond between a saccharide and a protein side chain can be through either a___ or a ____ atom. O or N
Created by: fallsummerspring
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