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27 Cards in this Set
- Front
- Back
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True or False Each individual polypeptide of collagen has a left-handed helix conformation. Consequently, the triple helix of collagen also has a left-handed helix conformation |
False |
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Scurvy is due to a lack of [a] which leads to a deficiency in the activity of the enzymes that [b] hydroxylates [c] and [d] amino acid residues in collagen. The enzymes involved require that the [e] oxidation state of iron in their prosthetic group is maintained. vitamin D, alanine, pretranslationally, ascorbic acid, ferric, proline, arginine, vitamin E, lysine, glycine, posttranslationally, ferrous, free iron, |
A- Ascorbic acid B- Post translationally C- Proline D- Lysine E-Ferrous |
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Fibril-associated collagen: A. connects collagen fibrils to other extracellular components. B. consists of beta sheets found in basement membranes C. has a rope-like structure found in bones and skin D. has a mesh-like structure found in basement membranes |
A |
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Fibril Forming collagen: A. connects collagen fibrils to other extracellular components. B. consists of beta sheets found in basement membranes C. has a rope-like structure found in bones and skin D. has a mesh-like structure found in basement membranes |
C |
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Network forming collagen: A. connects collagen fibrils to other extracellular components. B. consists of beta sheets found in basement membranes C. has a rope-like structure found in bones and skin D. has a mesh-like structure found in basement membranes |
D |
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This following specific disorder affects the enzyme lysyl hydroxylase and results in a defect in collagen synthesis that shows as 'strechy skin' in humans. A. Ehlers-Danlos syndrome B. Thalassemia C. Osteogenesis imperfecta type II D. Osteogenesis imperfecta type I |
A |
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True or False Ascorbic acid is necessary for the formation of hydroxyproline and hydroxylysine residues before they are incorporated into the collagen protein molecule. |
False |
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The α-keratin chains indicated by the diagram below have undergone one chemical step (Chemical reduction). To alter the shape of the α-keratin chains—as in hair waving—what subsequent steps are required in the following diagram? |
Shape remodelling then chemical oxidation |
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Which of the following statements is most likely NOT a property of collagen? A. much higher abundance of glu residues compared with most other proteins B. Hydroxylation of residues increases the stability of collagen by increasing hydrogen bonding between polypeptide chains C. Hydroxyproline and hydroxylysine residues are present D. The absence of significant levels of α-helical structure |
A |
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Match the fibous protien to the following charcteristics A. Strong and inelastic B. Strong, insoluble, and elastic C. Tough, insoluble structures of varying hardness and flexibility D. Soft, flexible, inelastic |
A- collagen B- elastase C-keratin D- fibroin |
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If most fibrous proteins are insoluble in water, at physiological pH and temperature, what would that tell you about their likely composition? A. There would be a high proportion of glutamate and aspartate residues in the proteins. B. There would be a high proportion of lysine and arginine residues in the proteins. C. There would be a high proportion of hydrophobic residues in the proteins. D. There would be a high proportion of hydrophilic residues in the proteins. E. There would be a high proportion of serine, threonine, and tyrosine residues in the proteins. |
C |
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There are at least 25 different 'types' of collagen. These types play a major role in the following locations in the human body: A. red blood cells B. tendons C. cornea of the eye D. plasma E. bone F. vitreous humor of the eye |
B C E and F |
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Fibrous proteins are strong or elastic and are insoluble in water. These characteristics and especially the insolubility means that: A. fibrous proteins have a high concentration of polar residues at the surface of the protein B. fibrous proteins have a high concentration of charged residues at the interior of the protein C. fibrous proteins have a high concentration of hydrophilic residues at the interior of the protein D. fibrous proteins have a high concentration of hydrophobic residues at the surface of the protein |
D |
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Which of the following are characteristics of collagen: A. Glycine makes up about on third of the amino acid composition B. Proline destablises the left hand helical structure of the collagen polypeptide chain C. Glycine and Alanine present the only R groups that can fit in the interior of the 3 stranded coil of collagen D. The triple helix in collagen has a right-handed conformation, whereas each individual chain has a left handed conformation |
A and D |
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The newly synthesised [a] is exported from the cell and subsequently cleaved by peptidases in the extracellular space to give [b].This then spontaneously associates to form [c]. |
A- procollagen B-tropocollagen C-Fibrils |
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Which of the following is the most likely post transitional modification of collagen: A. Residue: histidine. Modification: phosphorylation B. Residue: lysine. Modification: hydroxylation C. Residue: histidine. Modification: hydroxylation D. Residue: lysine. Modification: phosphorylation |
B |
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Which of the following are characteristics of fribrous proteins? A. Predominance of a single type of secondary structure usually repeated in a regular arrangement B. Hydrophobic residues in the interior of the protein residues C. Soluble in water D. 3D structural complexity of folded tertiary structure including secondary, tertiary and quaternary interactions |
A |
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Which fibrous protein has some interesting biotechnolgy applications? |
Fibroin |
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Which of the following statements is the most likely correct? A. Procollagen and proelastin are insoluble precursors of tropocollagen and elastin B. Elastin has a very high content of alanine C. Elastin is a rubber-like protein occuring predominantly in the skin D. Desmosine is a cross-link in mature collagen, derived from four lysine residues |
B |
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Which of the following is one of the most abundant proteins in the human body? A. collagen B. keratin C. fibroin D. myoglobin |
A |
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Statement:The alpha chain of collagen is like an alpha helix in globular proteins Reason:The alpha chain of collagen is stabilised by intrachain hydrogen bonds. |
Statement is True; Reason is False |
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Which of the following is the most likely post transitional modification of collagen: A. Residue: proline. Modification: glycosylation B. Residue: hydroxyproline. Modification: hydroxylation C. Residue: hydroxylysine. Modification: glycosylation D. Residue: lysine. Modification: phosphorylation |
C |
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Gelatin is derived from collagen and is used in cooking, cosmetics, and sweets (e.g. marshmallows). Gelatin can absorb a large amount of water and form gels. Consequently, gelatin is likely to be a: A. polysaccharide B. protein C. lipid D. nucelic acid |
Protein |
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How is fibroin structure different from collagen, keratin, or elastin? |
Fibroin has a high proportion of β-strands |
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The following specific disorder produces abnormal alpha chains of collagen and results in 'brittle bone' disease. A. Ehlers-Danlos syndrome B. Ehlers-Danlos syndrome type II C. Thalassemia type III D. Osteogenesis imperfecta type I |
D |
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Silk does not stretch but is flexible because: A. The peptide bond is rigid and planar B. Its structure is mostly beta sheet and strands C. The protein form a rod-like structure D. Its structure is mostly alpha helices |
B |
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Collagen is a: A. globular protein with three intertwined polypeptidechains B. fibrous protein with three intertwined polypeptidechains C. fibrous protein with three intertwined alpha-helixpolypeptide chains D. globular protein with three intertwined alpha-helixpolypeptide chains E. readily soluble protein |
B |
