69 Questions
What is a characteristic of proteins?
High molecular masses expressed in kDa
What is the general term for carbohydrates that are covalently bonded to other biomolecules?
Bioconjugates
What is the general term for lipids that show a dual nature with hydrophilic and lipophilic parts?
Amphiphilic lipids
What is the building block of nucleic acids?
Nucleotides
What is the term for lipids that are derived from phosphoric acids and esterified with fatty acids?
Phospholipids
What is the term used to describe the building blocks of larger molecules called polymers?
Monomers
Which of the following is an example of a polymer?
Polysaccharide
What is the term used to describe the study of the qualitative and quantitative analysis of biological activity and detection of biological molecules?
BioAnalytical Chemistry
Which of the following biomolecules includes lipids and derivatives?
Small molecules
What is the term used to describe the nitrogen-containing ring structure found in nucleotides?
Nitrogenous base
What is the primary function of insoluble carbohydrate polymers in cell walls?
To serve as structural and protective elements
What is the main difference between RNA and DNA in terms of stability?
DNA is more stable than RNA
What type of molecules are formed when carbohydrate polymers are covalently attached to proteins or lipids?
Glycoproteins
What comprises the lipophilic fraction of a biological sample?
Triglycerides, fatty acids, alcohols, sterols, and fat-soluble vitamins
What is the purpose of carbohydrate polymers in lubricating skeletal joints?
To reduce friction between moving joints
What is the process by which polysaccharides, nucleic acids, and proteins are formed?
Polymerization
What is the molecular weight of the monomers that make up macromolecules?
500 or less Da
What type of bond links amino acids together in proteins?
Peptide bond
What is the term for the complex formed by the assembly of macromolecules?
Supramolecular complex
What is the term for the end of a polypeptide chain?
C-terminal
What is the primary purpose of quenching metabolism in metabolomics?
To stop or slow down the metabolic process
Approximately what percentage of total dry mass in cells are proteins?
50%
What is the estimated number of different proteins in the human body?
100,000
What is the process that converts CO2 and H2O into cellulose and other plant products?
Photosynthesis
What is the term that describes the study of small molecules or metabolites within a biological sample?
Metabolomics
What is the primary source of carbohydrates in nature?
Plant products
What is the ratio of proteins to other macromolecules in cells?
5:1
What is the term that describes the extraction of metabolites from a biological sample?
Extraction
What is the importance of stopping or slowing down metabolism in highly metabolically active systems?
To prevent sample degradation
What percentage of the hemoglobin molecule's mass is made up of iron ions?
0.3%
What are the building blocks of DNA?
Nucleotides
What is the typical molecular weight range of small biomolecules in cells?
100 to 500 Da
Which of the following biomolecules are often polyfunctional, containing two or more different kinds of functional groups?
Many biomolecules
What is the term for large biomolecules composed of simpler subunits?
Macromolecules
What is the name of the biomolecule that is a carrier of acetyl groups in some enzymatic reactions?
Acetyl-CoA
What are the four major classes of biomolecules that are important for all living things?
Carbohydrates, lipids, proteins, and nucleic acids
What is the concentration range of small biomolecules in cells?
μmol to mmol
What is the characteristic of biomolecules in the aqueous phase of cells?
Polar or charged and water-soluble
What is the result of replacing hydrogen atoms with functional groups in hydrocarbons?
An increase in the variety of organic compounds
What is the main cause of denaturation of proteins?
pH changes, mercaptoethanol, detergents, urea/guanidine and heat
What is the term for the structure that conserves a native-like secondary structure content but without the tightly packed protein interior?
Molten globule
What is the reason why proline creates a bend in an α-helix?
All of the above
What is the type of protein structure that describes the completely folded and compacted polypeptide chain?
Tertiary (3°) structure
What is the function of molecular chaperones?
To restore proteins that have become misfolded
What is the type of protein that contains polypeptide chains organized approximately parallel along a single axis?
Fibrous protein
What is the result of heat-induced denaturation of proteins?
Exposure of non-polar segments to aqueous solvent
What is the term for the association of polypeptide chains?
Quaternary (4°) structure
What is the driving force behind the hydrophobic effect?
Decrease in entropy in water
What is the location of hydrophobic residues in globular proteins?
Inside the protein
What is the role of 2,3-BPG in hemoglobin?
Decreases the affinity of hemoglobin for oxygen
What is the role of chaperones in protein folding?
To guide misfolded regions back into place
What is the difference between myoglobin and hemoglobin?
Myoglobin binds 1 O2 molecule, while hemoglobin binds 4 O2 molecules
What is the consequence of protein misfolding?
Loss of biological activity
What is the purpose of hydrogen bonding in the β-pleated sheet?
To form a sheet-like structure
What is the term for the change in direction of a polypeptide chain?
β-Reverse turn
What is the effect of pH changes on proteins?
Denaturation of proteins
What is the characteristic of globular proteins?
They are soluble in water and have a spherical shape
What is the function of cryo-electron microscopy?
To study the structure of proteins using complex computational processing algorithms
What is the term for the non-covalent interactions that stabilize the tertiary structure of a protein?
Hydrogen bonds, electrostatic interactions, and hydrophobic interactions
What is the 1° structure of a protein?
The sequence of amino acids in a polypeptide chain
What type of bond is responsible for the formation of α-helices in proteins?
Hydrogen bond
What is the characteristic of the R groups of amino acids in an α-helix?
They stick outward from the α-helix
What is the distance between each turn of the α-helix?
5.4 Å
What is the number of amino acids per turn in an α-helix?
3.6
What type of structure is formed by a regular pattern of hydrogen bonds between the amide N-H and C=O groups of amino acids?
α-helix
Which bonds have free rotation in a protein?
Both of the above
What is the direction of the hydrogen bonds in an α-helix?
Parallel to the axis
What is the role of hydrogen bonds in the formation of an α-helix?
They pull the polypeptide chain into a helical structure
What is the sequence of amino acids in a polypeptide chain read from?
N-terminal end to C-terminal end
Learn about the basic characteristics of proteins, polysaccharides, and other biomolecules, including their molecular masses, isoelectric points, and bonding properties. Understand the foundation of biochemistry and how these molecules constitute cells.
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