CHAPTER 2 SUB QUESTION escribe the properties of carbon that make it well suited
ID: 187622 • Letter: C
Question
CHAPTER 2 SUB QUESTION
escribe the properties of carbon that make it well suited as a building block for biological molecules.
Discuss the stability of carbon covalent bonds and why these bonds are affected/or not affected by the thermal energy of molecules, the visible light spectrum, and the UV light spectrum.
Discuss why many of the functional groups commonly found in biological molecules are water soluble.
Describe the role of noncovalent bonds in maintaining the structure of molecules.
Explain the difference of polar vs. nonpolar molecules, discussing why/how polarity affects the solubility of molecules in water.
Explain the differences between oxidation and reduction reactions.
Explain the concept of stereoisomerism (do all carbon-containing molecules occur as stereoisomers, or are there certain characteristics that dictate this?), and discuss whether stereoisomers are equivalently used by cells.
Describe the properties of water that make it well suited as a biological solvent.
Describe the components of cellular membranes and explain how the structure of membrane phospholipids allows a lipid bilayer to spontaneously assemble in an aqueous environment.
Predict the permeability of lipid bilayers to different molecules (e.g., ions, nonpolar molecules, large and small polar molecules)
Explain why ions are unable to pass through a lipid bilayer unaided, and the types of proteins present in cellular membranes that aid in the transport of ions.
Describe the different macromolecules of the cell, explaining which of these molecules can be considered polymers and why, and discussing the diversity of the different macromolecules.
Explain the principles of stepwise polymerization from monomers.
Explain the principle of self-assembly, describing the evidence which supports that this principle applies to proteins, and discussing how the chemical properties of a macromolecule (e.g., the R groups of the amino acids that make up a polypeptide) drive the self-assembly process.
Describe the different types of covalent and non-covalent bonds that are important in protein folding (more on this in Lecture 3).
Describe the role of molecular chaperones in protein folding, particularly since proteins have the ability to self-assemble (more on this in Lecture 3).
Discuss why it is accepted that only 20 kinds of amino acids are involved in protein synthesis despite the presence of additional kinds of amino acids in some proteins.
Explain why the R group largely determines the properties of an amino acid.
Describe the three major types of amino acids, explaining the general chemical characteristics of each type, the types of bonds or interactions that each type can form, and where in a protein you would expect to find each type (also consider that some proteins have regions that are embedded in the cell membrane).
Describe the types of bonds that join amino acids together in polypeptides and explain how this relates to the directionality of proteins.
Explain the difference between a polypeptide and a protein
Explain the difference between a monomeric and a multimeric protein (more on this in Lecture 3).
escribe the properties of carbon that make it well suited as a building block for biological molecules.
Discuss the stability of carbon covalent bonds and why these bonds are affected/or not affected by the thermal energy of molecules, the visible light spectrum, and the UV light spectrum.
Discuss why many of the functional groups commonly found in biological molecules are water soluble.
Describe the role of noncovalent bonds in maintaining the structure of molecules.
Explain the difference of polar vs. nonpolar molecules, discussing why/how polarity affects the solubility of molecules in water.
Explain the differences between oxidation and reduction reactions.
Explain the concept of stereoisomerism (do all carbon-containing molecules occur as stereoisomers, or are there certain characteristics that dictate this?), and discuss whether stereoisomers are equivalently used by cells.
Describe the properties of water that make it well suited as a biological solvent.
Describe the components of cellular membranes and explain how the structure of membrane phospholipids allows a lipid bilayer to spontaneously assemble in an aqueous environment.
Predict the permeability of lipid bilayers to different molecules (e.g., ions, nonpolar molecules, large and small polar molecules)
Explain why ions are unable to pass through a lipid bilayer unaided, and the types of proteins present in cellular membranes that aid in the transport of ions.
Describe the different macromolecules of the cell, explaining which of these molecules can be considered polymers and why, and discussing the diversity of the different macromolecules.
Explain the principles of stepwise polymerization from monomers.
Explain the principle of self-assembly, describing the evidence which supports that this principle applies to proteins, and discussing how the chemical properties of a macromolecule (e.g., the R groups of the amino acids that make up a polypeptide) drive the self-assembly process.
Describe the different types of covalent and non-covalent bonds that are important in protein folding (more on this in Lecture 3).
Describe the role of molecular chaperones in protein folding, particularly since proteins have the ability to self-assemble (more on this in Lecture 3).
Discuss why it is accepted that only 20 kinds of amino acids are involved in protein synthesis despite the presence of additional kinds of amino acids in some proteins.
Explain why the R group largely determines the properties of an amino acid.
Describe the three major types of amino acids, explaining the general chemical characteristics of each type, the types of bonds or interactions that each type can form, and where in a protein you would expect to find each type (also consider that some proteins have regions that are embedded in the cell membrane).
Describe the types of bonds that join amino acids together in polypeptides and explain how this relates to the directionality of proteins.
Explain the difference between a polypeptide and a protein
Explain the difference between a monomeric and a multimeric protein (more on this in Lecture 3).
Explanation / Answer
1). Carbon is an important structural element of all the living beings because it can form the four bonds with the other elements, which is necessary for the formation of biomolecules. The carbon covalent bonds are highly stable, which makes it an important element of the biomolecules. The small size and low molecular weight of the carbon allow the enzymes to manipulate the chemical bonds of the carbon.