Quiz
Chapter 2. Protein Composition and Structure
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Fragen in diesem Quiz (35)
1What is the function of insulin?
- ATreat diabetes
- BProtein hormone
- Ccrucial to maintaining salt levels at appropriate levels
- Dcrucial to maintaining blood sugar at appropriate levels
2One of the key properties of proteins are?
- AProteins are perpendicular polymers composed of amino acids
- Bproteins have a wide variety of functional groups
- CProteins can not interact with one another and other macromolecules to form complexes
- DAll proteins are rigid and flexible
3A primary structure is ?
- AChains of amino acids in a specific sequence
- BEntire chains fold into well defined structures
- CAmino acids close to one another within a sequence can fold into regular structures
- DComposed of multiple polypeptide chains called subunits
4Alpha helix and beta strands are examples of secondary structures formed by adjacent alpha strands
- ARichtig
- BFalsch
5Globular proteins such as myoglobin is an example of primary, secondary, tertiary or quaternary structure?
- APrimary
- BSecondary
- CTertiary
- DQuaternary
6Hemoglobin is an example of a quaternary structure
- ARichtig
- BFalsch
7What are the functions of enzymes?
- ADegrades DNA
- BDegrades RNA
- CCatalyst
8Myofibrils is an example of a protein
- ARichtig
- BFalsch
9Four classes of amino acids are as followed: [blank_start]Hydrophobic[blank_end] amino acids, [blank_start]Polar[blank_end] amino acids, [blank_start]Positively[blank_end] charged amino acids, and [blank_start]Negatively[blank_end] charged amino acids
- AHydrophobic
- BPolar
- CPositively
- DNegatively
10What are the components of an amino acid?
- ACarbon
- BNitrogen
- CCarboxylic acid
- DAmino group
- ER group
- FL group
11Only the R isomer is found in proteins
- ARichtig
- BFalsch
12At neutral pH amino acids primarily exist in the [blank_start]zwitterions[blank_end] form
- Azwitterions
13Which amino acid is a hydrophobic amino acid?
- AGlycine
- BSerine
- CArginine
- DAspartic Acid
14Positively charged amino acids are
- AHistidine
- BTyrosine
- CLeucine
- DArginine
- EIsoleucine
- FLysine
15Polar amino acids are
- ASerine
- BValine
- CThreonine
- DTyrosine
- EGlutamine
- FCysteine
- GMethionine
- HAsparagine
16Negatively charged amino acids consist of [blank_start]Aspartic[blank_end] acid and [blank_start]Glutamic[blank_end] Acid
- AAspartic
- BGlutamic
17Phenylalanine, Tryptophan, and Methionine are examples of what amino acid?
- APolar
- BPositively charged
- CHydrophobic
- DNegatively charged
18Glycine, alanine, proline, valine and serine are examples of hydrophobic amino acids
- ARichtig
- BFalsch
19Peptide bonds are planar
- ARichtig
- BFalsch
20Amino acids are linked by
- Apeptide bonds to form Polypeptide chains
- Balpha helix
- Cbeta sheets
- Ddisulfide bonds
21Most proteins consist of [blank_start]50[blank_end] to [blank_start]2000[blank_end] amino acids
- A50
- B2000
22Polypeptide chain can be cross-linked by sulfide bonds
- ARichtig
- BFalsch
23Secondary structure
- APolypeptide chains that fold into regular structures such as alpha helix, and beta sheet
- BHemoglobin
- CMyoglobin
- DChains of amino acids in a specific sequence
24Alpha helix are
- ACoiled structures stabilized by intracain hydrogen bonds
- BStabilized by hydrogen bonds between polypeptide strands
- CNot as rod like, fully extended not tightly coiled
25Osteogenesis imperfecta
- ADefect in collagen, Brittle bone disease occurs if a mutation results in the substitution of another amino acid in place of glycine
- Black of vitamin C preventing hydroxylation of collagen leading to abnormalities in collagen
- Cabsence of vitamin K leading to proteins not being carboxylated
26Tertiary structure
- ARefers to spatial arrangement of amino acids that are far apart in the primary structure and to the pattern of disulfide bond formation
- BCan be as simple as two identical polypeptide chains or as complex as dozens of different polypeptide chains
- CThree-dimensional structure formed by hydrogen bonds between peptide NH and CO groups of amino acids that near one another in the primary structure
27Keratin and collagen are examples of fibrous proteins
- ARichtig
- BFalsch
28Myoglobin is found within your [blank_start]muscle[blank_end] and [blank_start]binds oxygen[blank_end] on your muscle
- Amuscle
- Bbinds oxygen
29Quaternary structure
- AHemoglobin
- BGlobular proteins
- CSpatial arrangement of subunits and their nature of their interaction
- DSpatial arrangement of amino acids that are far apart in the primary structure
- EStructure assemble with other chains to form arrays such as the complex of six insulin molecules
- FMyoglobin
30Hemoglobin is an example of tertiary structure?
- ARichtig
- BFalsch
31Proteins can be denatured by any treatment that disrupts the weak bonds stabilizing tertiary structure such as
- AHeating
- BDenaturants
32Scurvy is an example of a disease that results from dysfunctional protein modification and is due to?
- ALack of vitamin D which prevents hydroxylation of collagen
- BLack of vitamin C which prevents hydroxylation of collagen leading to abnormalities in collagen
- Cdue to absence of vitamin K leading to clotting proteins not being carboxylated
33Hemorrhaging is due to the absence of vitamin K
- ARichtig
- BFalsch
34Amyloidoses plaques cause disease such as
- AAlzheimer's
- BParkinson's
- CHuntington's
- DHIV
- EOsteogenesis imperfecta
- FSickle cell
35The function of a promoter is to initiate process or transcription
- ARichtig
- BFalsch
Informationen
- Beschreibung
- Biochemistry
- Autor
- Amy Arce
- Sprache
- English
- Aufrufe
- 81
- Schlagwörter
- Bewertung
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