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