Podcast
Questions and Answers
What four kinds of molecules are characteristic of living things?
What four kinds of molecules are characteristic of living things?
Carbohydrates, lipids, proteins, and nucleic acids.
Which are considered polymers? of which monomers do they consist?
Which are considered polymers? of which monomers do they consist?
Carbohydrates are polymers consisting of monosaccharides. Proteins are polymers consisting of amino acids. Nucleic acids are polymers consisting of nucleotides.
What are the eight functional groups introduced in lecture?
What are the eight functional groups introduced in lecture?
Hydroxyl, carbonyl, carboxyl, amino, sulfhydryl, phosphate, methyl and aldehyde.
What are their names, chemical formulas, and important properties? i.e., which are polar? nonpolar? charged? acidic? basic?
What are their names, chemical formulas, and important properties? i.e., which are polar? nonpolar? charged? acidic? basic?
What is an isomer?
What is an isomer?
What are the three types of isomers presented in lecture?
What are the three types of isomers presented in lecture?
What occurs in a condensation reaction? a hydrolysis reaction?
What occurs in a condensation reaction? a hydrolysis reaction?
Proteins are polymers composed of which type of monomer?
Proteins are polymers composed of which type of monomer?
Which two functional groups are present in all amino acids?
Which two functional groups are present in all amino acids?
In which forms do these groups exist in amino acids found inside cells?
In which forms do these groups exist in amino acids found inside cells?
Which isomer form of amino acids do we observe in organisms?
Which isomer form of amino acids do we observe in organisms?
Which amino acids are positively charged?
Which amino acids are positively charged?
What does their charge mean for the chemical reactivity?
What does their charge mean for the chemical reactivity?
Which amino acids are uncharged but polar?
Which amino acids are uncharged but polar?
What does their polarity mean for the chemical reactivity?
What does their polarity mean for the chemical reactivity?
Which amino acids are nonpolar?
Which amino acids are nonpolar?
Which amino acids are exceptional and do not fall into the above three groups?
Which amino acids are exceptional and do not fall into the above three groups?
What is a disulfide bridge? which amino acid can form them?
What is a disulfide bridge? which amino acid can form them?
How do the size and shape of glycine and proline affect their location within a folded polypeptide?
How do the size and shape of glycine and proline affect their location within a folded polypeptide?
What distinguishes a "polypeptide" from a "peptide"?
What distinguishes a "polypeptide" from a "peptide"?
How is a peptide bond formed?
How is a peptide bond formed?
What comprises the primary structure of a protein?
What comprises the primary structure of a protein?
Which type(s) of bond is/are involved?
Which type(s) of bond is/are involved?
What comprises the secondary structure of a protein?
What comprises the secondary structure of a protein?
Flashcards
Four main classes of biomolecules:
Four main classes of biomolecules:
Carbohydrates, lipids, proteins, and nucleic acids.
What is an isomer?
What is an isomer?
Molecules with the same molecular formula but different structures and properties.
Three types of isomers:
Three types of isomers:
Structural isomers, cis-trans isomers, and enantiomers.
Condensation reaction
Condensation reaction
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Monomer of proteins:
Monomer of proteins:
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Two functional groups in amino acids:
Two functional groups in amino acids:
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Amino acid isomer in organisms:
Amino acid isomer in organisms:
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Primary Protein Structure:
Primary Protein Structure:
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Secondary Protein Structure:
Secondary Protein Structure:
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Amino acid that forms disulfide bridges:
Amino acid that forms disulfide bridges:
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Study Notes
- The four kinds of molecules that are characteristic of living things include carbohydrates, lipids, proteins, and nucleic acids.
- Polymers include carbohydrates, proteins, and nucleic acids
- Carbohydrates are made of monosaccharides
- Proteins are made of amino acids
- Nucleic acids are made of nucleotides
- Eight functional groups are important in biology:
- Hydroxyl (-OH): polar due to electronegative oxygen
- Carbonyl (>C=O): polar; ketones and aldehydes
- Carboxyl (-COOH): acidic; can donate H+
- Amino (-NH2): basic; can accept H+
- Sulfhydryl (-SH): can form disulfide bridges
- Phosphate (-OPO3^2-): contributes negative charge
- Methyl (-CH3): nonpolar; affects gene expression
- Isomers are molecules with the same molecular formula but different structures and properties.
- Three types of isomers include:
- Structural isomers: different covalent arrangements
- Cis-trans isomers: different arrangement around a double bond
- Enantiomers: mirror images of each other
- A condensation reaction is a reaction in which two molecules are covalently bonded to each other through the loss of a small molecule, usually water
- A hydrolysis reaction is a reaction in which a molecule is broken down by the addition of water.
- Proteins are polymers composed of amino acids.
- Two functional groups present in all amino acids include an amino group (-NH2) and a carboxyl group (-COOH).
- These groups exist in the ionized form in amino acids inside cells
- The L isomer of amino acids is observed in organisms.
- Positively charged (basic) amino acids include:
- Lysine
- Arginine
- Histidine
- Positive charge allows them to form ionic bonds with negatively charged molecules or participate in acid-base catalysis.
- Negatively charged (acidic) amino acids include:
- Aspartic acid
- Glutamic acid
- Negative charge allows them to form ionic bonds with positively charged molecules or participate in acid-base catalysis.
- Uncharged polar amino acids include:
- Serine
- Threonine
- Cysteine
- Tyrosine
- Asparagine
- Glutamine
- Polarity allows them to form hydrogen bonds with other polar molecules.
- Nonpolar amino acids
- Glycine
- Alanine
- Valine
- Leucine
- Isoleucine
- Methionine
- Phenylalanine
- Tryptophan
- Proline
- Nonpolarity causes them to cluster together in the interior of proteins, away from water
- Exceptional amino acids are:
- Cysteine
- Glycine
- Proline
- A disulfide bridge is a covalent bond between the sulfur atoms of two cysteine residues.
- Size and shape of glycine and proline:
- Glycine: small, achiral, increases flexibility in polypeptide chains
- Proline: rigid, cyclic structure, introduces kinks in polypeptide chains
- A polypeptide is a polymer of many amino acids linked by peptide bonds, while a peptide is a short chain of amino acids.
- A peptide bond is formed through a condensation reaction between the carboxyl group of one amino acid and the amino group of another amino acid.
- The primary structure of a protein is comprised of the sequence of amino acids linked by peptide bonds.
- Peptide bonds are involved in the primary structure of a protein
- The secondary structure of a protein comprises local folding patterns such as alpha helices and beta sheets, stabilized by hydrogen bonds between atoms of the polypeptide backbone.
- Hydrogen bonds are involved in the secondary structure of a protein
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