Protein - Quiz
A) Electrophoresis B) Ultracentrifugation C) Cell lysis D) Salting out
A) Crude lysate B) Buffer C) Matrix D) Supernatant
A) Site-directed mutagenesis B) GFP fusion C) Salting out D) His-tagging
A) Luminescence B) Fluorescence C) Binding affinity D) Density
A) Spectroscopy B) Gel electrophoresis C) Enzyme assays D) Mass spectrometry
A) Green fluorescent protein B) Nickel ions C) Modified tRNAs D) Histidine residues
A) Sucrose B) Nickel C) Gold D) Antibodies
A) Cytoplasm B) Nucleus C) Mitochondria D) Endoplasmic reticulum
A) Nickel B) Histidine residues C) Gold D) Green fluorescent protein
A) Immunohistochemistry B) Fluorescent microscopy C) Immunoelectron microscopy D) Isopycnic centrifugation
A) Sucrose B) Nickel C) Gold D) Copper
A) Ultracentrifugation B) Site-directed mutagenesis C) Electrophoresis D) Cofractionation
A) Gold particles B) Nickel ions C) Green fluorescent protein D) Unnatural amino acids
A) Isopycnic centrifugation B) Electrophoresis C) Salting out D) Immunohistochemistry
A) Luminescent or chromogenic signals B) Atomic mass C) Density measurements D) Enzymatic inhibition
A) Quinary structure B) Native conformation C) Primary sequence D) Denatured state
A) Enzymes B) Substrates C) Dehydrons D) Molecular chaperones
A) A lipid B) A polysaccharide C) A nucleic acid D) A polyamide
A) Hydrophobic repulsion B) Covalent bonds C) Hydrogen bonds D) Ionic interactions
A) Protein subunit B) Alpha-helix C) Hydrophobic core D) Disulfide bridge
A) Tertiary structure B) Secondary structure C) Primary structure D) Quinary structure
A) Subunit B) Sequence C) Conformation D) Fold
A) Tertiary structure B) Quaternary structure C) Secondary structure D) Quinary structure
A) Catalysts B) Subunits C) Chaperones D) Dehydrons
A) The crowded cellular interior B) The amino acid sequence C) The internal hydrophobic core D) The membrane channels
A) Catalytic sequences B) Conformational changes C) Dehydration D) Subunit folding
A) Quinary surface B) Molecular chaperone C) Hydrophobic core D) Active site
A) Structural proteins B) Fibrous proteins C) Membrane proteins D) Globular proteins
A) Hemoglobin B) Lipase C) Collagen D) Receptor
A) Catalytic enzymes B) Hair and nail structure C) Receptors and channels D) Cellular interior organization
A) Molecular chaperones that assist folding B) Types of quaternary subunits C) Intramolecular hydrogen bonds poorly shielded from water D) A class of fibrous proteins
A) Lack of primary structure B) Constant synthesis of new amino acids C) Thermal vibration and collisions D) Presence of molecular chaperones
A) Hydrophobic core B) Thermal energy C) Peptide bonds D) Polyamide bonding
A) Carl von Voit B) Jöns Jacob Berzelius C) Gerardus Johannes Mulder D) Antoine Fourcroy
A) 1747 B) 1789 C) 1862 D) 1838
A) Antoine Fourcroy B) Karl Heinrich Ritthausen C) Jöns Jacob Berzelius D) Gerardus Johannes Mulder
A) Biological B) Structural C) Essential D) Primary
A) Threonine B) Glycine C) Leucine D) Glutamic acid
A) Flesh makes flesh B) Proteins are toxic C) Proteins only exist in plants D) Proteins are unimportant for growth
A) Thomas Burr Osborne B) Lafayette Mendel C) William Cumming Rose D) Karl Heinrich Ritthausen
A) Leucine B) Glutamic acid C) Threonine D) Albumin
A) William Cumming Rose B) Thomas Burr Osborne C) Lafayette Mendel D) Gerardus Johannes Mulder
A) Armour Hot Dog Company B) German Nutritional Research Center C) Swedish Chemistry Institute D) Connecticut Agricultural Experiment Station
A) Peptides B) Amino acids C) Albumins D) Enzymes
A) A polysaccharide B) A polypeptide C) A nucleotide D) A proteasome
A) More than 20–30 B) Exactly 2 C) Exactly 5 D) Less than 10
A) 20 B) 10 C) 100 D) 50
A) Protein turnover B) Post-translational modification C) Genetic replication D) Peptide folding
A) Substrates B) Ligases C) Polypeptides D) Cofactors
A) 1–2 minutes B) 1–2 hours C) 1–2 years D) 1–2 days
A) Ribosome B) Nucleus C) Proteasome D) Mitochondria
A) Polysaccharide B) Pyrrolysine C) Selenocysteine D) Ubiquitin ligases
A) Christian Anfinsen B) Linus Pauling C) Frederick Sanger D) Hermann Emil Fischer
A) Hemoglobin B) RNA polymerase C) Urease D) Ribonuclease A
A) Max Perutz B) Frederick Sanger C) Roger Kornberg D) Kaj Linderstrøm-Lang
A) Insulin B) Myoglobin C) Hemoglobin D) Ribonuclease A
A) 1949 B) 1972 C) 1958 D) 1999
A) Insulin B) Hemoglobin C) Ribonuclease A D) Urease
A) Maximum entropy B) Free energy minimum C) Highest potential energy D) A random coil state
A) Ribonuclease A B) RNA polymerase C) Urease D) Insulin
A) EC number system B) Gene ontology C) Protein Data Bank D) X-ray crystallography
A) Molecular weight B) Amino acid sequence length C) Number of disulfide bonds D) Intracellular location
A) Leucine B) Proline C) Glycine D) Alanine
A) Ligand B) Subunit C) Monomer D) Residue
A) Hydrophobic interactions B) Van der Waals forces C) Hydrogen bonding D) Resonance forms
A) Beta terminus B) N-terminus C) C-terminus D) Alpha terminus
A) Alphabetical order B) N-terminus to C-terminus C) Smallest residue to largest residue D) C-terminus to N-terminus
A) Base terminus B) N-terminus C) C-terminus D) Alpha terminus
A) Peptide resonance B) Dihedral angles C) The number of peptide bonds D) Ribosome synthesis speed
A) Aminoacyl tRNA synthetase B) RNA polymerase C) Titin D) RuBisCO
A) DNA replication B) Ribosome assembly C) Incorporating carbon dioxide into organic matter D) Synthesizing amino acids
A) 20,000 B) 50 million C) 6,000 D) 2 million
A) Amino acids B) Codons C) Nucleosides D) Anticodons
A) Methionine B) Alanine C) Titin D) Valine
A) 100 B) 20 C) 4 D) 64
A) In the cytoplasm B) In the nucleoid C) On the nuclear membrane D) In the cell nucleus
A) Translation B) Post-transcriptional modification C) Replication D) Transcription
A) Titin B) Ribosome C) RNA polymerase D) Aminoacyl tRNA synthetase
A) Dalton B) Gram C) Liter D) Nucleotide
A) Mycoplasma proteins B) Ribosomes C) RNA polymerases D) Titins
A) 31 kDa B) 49 kDa C) 53 kDa D) 3000 kDa
A) In the muscle sarcomere B) In the bacterial cell wall C) In the nucleus D) In the cytoplasm
A) Gel electrophoresis B) Mass spectrometry C) Chemical ligation D) Protein folding
A) Chromatographic separation B) Oxidative phosphorylation C) Thermal denaturation D) Genetic engineering
A) It is not suitable for such purposes B) It produces toxic byproducts C) It is too fast for assembly lines D) It requires radioactive materials
A) It occurs simultaneously B) It is the same C) It is opposite D) It is unrelated
A) DNA replication B) Lipid storage C) Cell wall reinforcement D) Kinase activity
A) PxxP motifs B) Lipid membranes C) Ribosomal RNA D) DNA sequences
A) The Human Genome Project B) The Ribosome database C) Eukaryotic Linear Motif (ELM) database D) The Protein Data Bank
A) 3% B) 75% C) 50% D) 20%
A) Genome B) Proteome C) Transcriptome D) Metabolome
A) Only during protein synthesis B) Only in plant cells C) Yes D) No, they are permanent
A) Receptors B) Antigens C) Ligands D) Substrates
A) Haemoglobin B) Insulin C) A dirigent protein D) A plasma cell
A) Sugar moieties B) Oxygen C) DNA D) Potassium ions
A) Plasma cells B) Stem cells C) Lung cells D) Liver cells
A) Providing rigid structural support B) Generating mechanical forces C) Regulating gene expression D) Synthesizing DNA
A) Dynein B) Collagen C) Elastin D) Keratin
A) The endoplasmic reticulum B) The cytoskeleton C) The cell membrane D) The nuclear envelope
A) X-ray crystallography B) Gel electrophoresis C) DNA sequencing D) Polymerase chain reaction |
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