role of non bonding interaction in structure and function of macro molecules
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Biological macromolecules are large and complex
Macromolecules are made up of basic molecular units. They include the proteins (polymers of amino acids), nucleic acids (polymers of nucleotides), carbohydrates (polymers of sugars) and lipids (with a variety of modular constituents). The biosynthesis and degradation of biological macromolecules involves linear polymerization, breakdown steps (proteins, nucleic acids and lipids) and may also involve branching/debranching (carbohydrates). These processes may involve multi-protein complexes (e.g. ribosome, proteasome) with complex regulation.
Associated learning goals
• Students should be able to discuss the diversity and complexity of various biologically relevant macromolecules and macromolecular assemblies in terms of evolutionary fitness. {A}
• Students should be able to describe the basic units of the macromolecules and the types of linkages between them. {A}
• Students should be able to compare and contrast the processes involved in the biosynthesis of the major types of macromolecules (proteins, nucleic acids and carbohydrates). {B}
• Students should be able to compare and contrast the processes involved in the degradation of the major types of macromolecules (proteins, nucleic acids and carbohydrates.{B}
• Students should understand that proteins are made up of domains and be able to discuss how the protein families arise from duplication of a primordial gene. {C}
2. Structure is determined by several factors
Covalent and non-covalent bonding govern the three dimensional structures of proteins and nucleic acids which impacts function. The amino acid sequences observed in nature are highly selected for biological function but do not necessarily adopt a unique folded structure. The structure (and hence function) of macromolecules is governed by foundational principles of chemistry such as: covalent bonds and polarity, bond rotations and vibrations, non-covalent interactions, the hydrophobic effect and dynamic aspects of molecular structure. The sequence (and hence structure and function) of proteins and nucleic acids can be altered by alternative splicing, mutation or chemical modification. Sequences (and hence structure and function) of macromolecules can evolve to create altered or new biological activities.
Associated learning goals
• Students should be able to recognize the repeating units in biological macromolecules and be able to discuss the structural impacts of the covalent and noncovalent interactions involved. {A}
• Students should be able to discuss the composition, evolutionary change and hence structural diversity of the various types of biological macromolecules found in organisms. {A}
• Students should be able to discuss the chemical and physical relationships between composition and structure of macromolecules. {A}
• Students should be able to compare and contrast the primary, secondary, tertiary and quaternary structures of proteins and nucleic acids. {B}
• Students should be able to use various bioinformatics approaches to analyze macromolecular primary sequence and structure. {B}
• Students should be able to compare and contrast the effects of chemical modification of specific amino acids on a three dimensional structure of a protein. {B}
• Students should be able to compare and contrast the ways in which a particular macromolecule might take on new functions through evolutionary changes. {B}
• Students should be able to use various bioinformatics and computational approaches to compare primary sequences and identify the impact of conservation and/or evolutionary change on the structure and function of macromolecules. {C}
• Students should be able to predict the effects of mutations on the activity, structure or stability of a protein and design appropriate experiments to assess the effects of mutations. {C}
• Students should be able to propose appropriate chemical or chemical biology approaches to explore the localization and interactions of biologic
Macromolecules are made up of basic molecular units. They include the proteins (polymers of amino acids), nucleic acids (polymers of nucleotides), carbohydrates (polymers of sugars) and lipids (with a variety of modular constituents). The biosynthesis and degradation of biological macromolecules involves linear polymerization, breakdown steps (proteins, nucleic acids and lipids) and may also involve branching/debranching (carbohydrates). These processes may involve multi-protein complexes (e.g. ribosome, proteasome) with complex regulation.
Associated learning goals
• Students should be able to discuss the diversity and complexity of various biologically relevant macromolecules and macromolecular assemblies in terms of evolutionary fitness. {A}
• Students should be able to describe the basic units of the macromolecules and the types of linkages between them. {A}
• Students should be able to compare and contrast the processes involved in the biosynthesis of the major types of macromolecules (proteins, nucleic acids and carbohydrates). {B}
• Students should be able to compare and contrast the processes involved in the degradation of the major types of macromolecules (proteins, nucleic acids and carbohydrates.{B}
• Students should understand that proteins are made up of domains and be able to discuss how the protein families arise from duplication of a primordial gene. {C}
2. Structure is determined by several factors
Covalent and non-covalent bonding govern the three dimensional structures of proteins and nucleic acids which impacts function. The amino acid sequences observed in nature are highly selected for biological function but do not necessarily adopt a unique folded structure. The structure (and hence function) of macromolecules is governed by foundational principles of chemistry such as: covalent bonds and polarity, bond rotations and vibrations, non-covalent interactions, the hydrophobic effect and dynamic aspects of molecular structure. The sequence (and hence structure and function) of proteins and nucleic acids can be altered by alternative splicing, mutation or chemical modification. Sequences (and hence structure and function) of macromolecules can evolve to create altered or new biological activities.
Associated learning goals
• Students should be able to recognize the repeating units in biological macromolecules and be able to discuss the structural impacts of the covalent and noncovalent interactions involved. {A}
• Students should be able to discuss the composition, evolutionary change and hence structural diversity of the various types of biological macromolecules found in organisms. {A}
• Students should be able to discuss the chemical and physical relationships between composition and structure of macromolecules. {A}
• Students should be able to compare and contrast the primary, secondary, tertiary and quaternary structures of proteins and nucleic acids. {B}
• Students should be able to use various bioinformatics approaches to analyze macromolecular primary sequence and structure. {B}
• Students should be able to compare and contrast the effects of chemical modification of specific amino acids on a three dimensional structure of a protein. {B}
• Students should be able to compare and contrast the ways in which a particular macromolecule might take on new functions through evolutionary changes. {B}
• Students should be able to use various bioinformatics and computational approaches to compare primary sequences and identify the impact of conservation and/or evolutionary change on the structure and function of macromolecules. {C}
• Students should be able to predict the effects of mutations on the activity, structure or stability of a protein and design appropriate experiments to assess the effects of mutations. {C}
• Students should be able to propose appropriate chemical or chemical biology approaches to explore the localization and interactions of biologic
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