A collagenopathy:A. results in production of abnormal beta sheet proteinsB. is a hereditary genetic disorderC. may result from a deficiency of enzymes D. is a communicable disease (i.e. can be passed on from one person to another)

B. is a hereditary genetic disorderC. may result from a deficiency of enzymes

There are at least 25 different 'types' of collagen. These types play a major role in the following locations in the human body:A. cornea of the eyeB. tendonsC. plasmaD. red blood cellsE. boneF. vitreous humor of the eye

cornea of the eyetendonsbonevitreous humor of the eye

BCCB2000 Lecture 7 Questions Flashcards by Ana Lis

Which of the following are characteristics of fibrous proteins? A. Compact shapes including ‘spherical’ shape B. Comprised of a mix of secondary structures interacting in various ways C. Extended polypeptide chains forming long strands or ‘sheets’ D. Provide shape, strength, support, flexibility, and protection of the cell

C. Extended polypeptide chains forming long strands or ‘sheets’ D. Provide shape, strength, support, flexibility, and protection of the cell

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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. protein B. nucelic acid C. lipid D. polysaccharide

A. protein

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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. fibrous protein with three intertwined polypeptidechains

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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 I D. Osteogenesis imperfecta type II

A. Ehlers-Danlos syndrome

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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.

Specified Answer for: a ascorbic acid Specified Answer for: b postranslationally Specified Answer for: c lysine Specified Answer for: d proline Specified Answer for: e ferrous

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Each individual polypeptide of collagen has a left-handed helix conformation. Consequently, the triple helix of collagen also has a left-handed helix conformation. True or False?

False

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The α-keratin chains indicated by the diagram below have undergone one chemical step. To alter the shape of the α-keratin chains—as in hair waving—what subsequent steps are required in the following diagram? A. chemical reduction and then chemical oxidation B. chemical oxidation and then shape remodeling C. shape remodeling and then chemical reduction D. shape remodeling and then chemical oxidation E. chemical reduction and then shape remodeling

D. shape remodeling and then chemical oxidation

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A post-translational modification is an alteration that occurs to a protein after it has been translated. This alteration occurs at one, or more, residues within the protein. The following options show both a residue and a possible modification. Select the most option that describes the most likely post-translational modification that occurs in collagen. A. Residue: lysine. Modification: hydroxylation B. Residue: histidine. Modification: phosphorylation C. Residue: histidine. Modification: hydroxylation D. Residue: lysine. Modification: phosphorylation

A. Residue: lysine. Modification: hydroxylation

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Ascorbic acid is necessary for the formation of hydroxyproline and hydroxylysine residues before they are incorporated into the collagen protein molecule. True or False?

False

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Silk does not stretch but is flexible because: A. Its structure is mostly alpha helices B. The peptide bond is rigid and planar C. The protein form a rod-like structure D. Its structure is mostly beta sheet and strands

D. Its structure is mostly beta sheet and strands

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A collagenopathy: A. results in production of abnormal beta sheet proteins B. is a hereditary genetic disorder C. may result from a deficiency of enzymes D. is a communicable disease (i.e. can be passed on from one person to another)

B. is a hereditary genetic disorder C. may result from a deficiency of enzymes

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Which of the following are characteristics of the globular protein myoglobin? A. Predominance of a single type of secondary structure usually repeated in a regular arrangement B. Soluble in water C. 3D structural complexity of folded tertiary structure including secondary, tertiary and quaternary interactions D. Extended polypeptide chains forming long strands or ‘sheets’

B. Soluble in water C. 3D structural complexity of folded tertiary structure including secondary, tertiary and quaternary interactions

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Which of the following are characteristics of fibrous proteins? A. Predominance of a single type of secondary structure usually repeated in a regular arrangement B. 3D structural complexity of folded tertiary structure including secondary, tertiary and quaternary interactions C. Hydrophobic residues in the interior of the protein residues D. Soluble in water

A. Predominance of a single type of secondary structure usually repeated in a regular arrangement

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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. cornea of the eye B. tendons C. plasma D. red blood cells E. bone F. vitreous humor of the eye

cornea of the eye tendons bone vitreous humor of the eye

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Which of the following are characteristics of collagen: A. The triple helix in collagen has a right-handed conformation, whereas each individual chain has a left handed conformation B. Glycine makes up about on third of the amino acid composition C. Glycine and Alanine present the only R groups that can fit in the interior of the 3 stranded coil of collagen D. Proline destablises the left hand helical structure of the collagen polypeptide chain

A. The triple helix in collagen has a right-handed conformation, whereas each individual chain has a left handed conformation B. Glycine makes up about on third of the amino acid composition

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Which of the following statements is most likely NOT a property of collagen? A. 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

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A. A much higher abundance of glu residues compared with most other proteins

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

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B. Elastin has a very high content of alanine

Fibril-forming collagen: A. connects collagen fibrils to other extracellular components. B. has a rope-like structure found in bones and skin C. consists of beta sheets found in basement membranes D. has a mesh-like structure found in basement membranes

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B. has a rope-like structure found in bones and skin

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.

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C. There would be a high proportion of hydrophobic residues in the proteins.

This particular type of fibrous protein has some interesting biotechnology applications: A. Keratin B. Collagen C. Elastase D. Fibroin

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D. Fibroin

Three examples of fibrous proteins you learned from your lecture or texbook are: 1. [a] 2. [b] 3. [c]

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alpha keratin fibroin collagen silk fibroin keratin elastin

Determine of the statement and reason are correct, and if the reason matches the statement. 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.

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Statement is False; Reason is True

Which of the following are characteristics of fibrous proteins? A. Extended polypeptide chains forming long strands or ‘sheets’ B. Compact shapes including ‘spherical’ shape C. Comprised of a mix of secondary structures interacting in various ways D. Provide shape, strength, support, flexibility, and protection of the cell

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A. Extended polypeptide chains forming long strands or ‘sheets’ D. Provide shape, strength, support, flexibility, and protection of the cell

The structure of a protein is closely related to its physical characteristics and its function. A. α helix cross-linked by disulphide bonds (e.g. keratin) B. β strands and sheets (e.g. fibroin) C. triple helix (e.g. collagen) D. α helix and β conformation (e.g. elastase)

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A. Tough, insoluble structures of varying hardness and flexibility B. Soft, flexible, inelastic C. Strong and inelastic D. Strong, insoluble, and elastic

How is fibroin structure different from collagen, keratin, or elastin?

A. Fibroin has high proportion of α-strands
B. Fibroin has a high proportion of β-strands
C. Fibroin is synthesised from β-amino acids
D. Fibroin has a 'coiled coil' structure

B. Fibroin has a high proportion of β-strands

Which of the following is one of the most abundant proteins in the human body

A. collagen
B. myoglobin
C. keratin
D. fibroin

A. collagen

Which of the following are characteristics of collagen structure?

A. three intertwined α-polypeptide chains called a 'coiled coil'
B. Gly-X-Y repeating unit where X is often Pro and Y is often 4-Hydroxyproline
C. 4-hydroxyproline and 4-hydroxylysine form intermolecular hydrogen bonds
D. A and B above
E. A, B, and C above

E. A, B, and C above

BCCB2000 Lecture 7 Questions Flashcards

(27 cards)