Introduction to Proteins
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Questions and Answers

What are the macromolecules that are considered polymers? What is an example of a non-polymeric chained macromolecule? What's the distinction?

Proteins, nucleic acids, carbohydrates, and lipids. Lipids are not polymers because they are not formed from repeating monomer units. Polymers are chains of repeating monomer units, while non-polymers are not.

What are the 9 main functions (classes) of proteins?

Enzymes, structural proteins, storage proteins, transport proteins, hormonal proteins, receptor proteins, contractile and motor proteins, defensive proteins, and toxins.

Draw by hand from scratch the common structure that all amino acids share, using “R” in your picture to generically represent the side chain.

The common structure includes a central carbon atom bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (-H), and an R-group (side chain).

How can you identify all 20 amino acid side chains if shown to you as a stick-figure molecule?

<p>By recognizing the unique structure and chemical properties of each side chain.</p> Signup and view all the answers

How can you determine whether an amino acid is polar/nonpolar, charged/uncharged, hydrophilic/hydrophobic?

<p>By examining the chemical structure of the side chain; polar side chains contain electronegative atoms (O, N) or are charged, while nonpolar side chains are mostly composed of carbon and hydrogen.</p> Signup and view all the answers

What are the 3 letter and 1 letter abbreviations used for amino acids?

<p>Each amino acid has a unique 3-letter and 1-letter abbreviation (e.g., Alanine: Ala, A).</p> Signup and view all the answers

What are peptide bonds? Which parts of the amino acid molecule participate in adding to the elongating polypeptide backbone?

<p>Peptide bonds are covalent bonds formed between the carboxyl group of one amino acid and the amino group of another. The carboxyl group and amino group participate in forming peptide bonds.</p> Signup and view all the answers

When do we call an amino acid a “residue”? Why is this name appropriate?

<p>When it is incorporated into a polypeptide chain. The name is appropriate because part of the amino acid molecule (H2O) is 'left behind' or 'remains' after the peptide bond is formed.</p> Signup and view all the answers

When a folded protein is shown as a squiggly line drawing, what does this represent? What parts are omitted for clarity?

<p>The squiggly line represents the path of the polypeptide backbone. All the amino acid side chains are omitted for clarity.</p> Signup and view all the answers

What are the four types of side chain-to-side chain bonds involved in protein folding? Why are some stronger than others?

<p>Hydrogen bonds, ionic bonds, disulfide bridges, and van der Waals interactions. Covalent bonds, such as disulfide bridges, are stronger than non-covalent interactions like hydrogen bonds, ionic bonds, and Van der Waals interactions.</p> Signup and view all the answers

Understand what is meant by the Primary, Secondary, Tertiary, and (sometimes) Quaternary structure of proteins.

<p>Primary structure: the sequence of amino acids. Secondary structure: local folding patterns like alpha helices and beta sheets. Tertiary structure: the overall three-dimensional shape of a single polypeptide chain. Quaternary structure: the arrangement of multiple polypeptide chains in a multi-subunit protein.</p> Signup and view all the answers

Flashcards

Macromolecules that are polymers

Large molecules made of repeating structural units, like proteins and carbohydrates.

Example of non-polymeric macromolecule

Lipids are macromolecules that do not form polymers.

Functions of proteins

Proteins serve 9 main functions, including enzymes, structural support, and transport.

Common structure of amino acids

All amino acids share a central carbon, an amino group, a carboxyl group, and a variable side chain (R).

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Identify amino acid side chains

Recognizing different amino acids by their unique side chain structures.

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Amino acid properties

Amino acids can be classified as polar/nonpolar and charged/uncharged based on their side chains.

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Amino acid abbreviations

Each amino acid has unique three-letter and one-letter codes for identification.

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Peptide bonds

Covalent bonds formed between the amino group of one amino acid and the carboxyl group of another.

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Amino acid 'residue'

The term 'residue' refers to an amino acid within a polypeptide chain after the water molecule is removed.

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Folded protein representation

In diagrams, a squiggly line shows the backbone of a protein, often omitting side chains for clarity.

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Protein folding bonds

Four bond types: hydrogen, ionic, disulfide, and hydrophobic interactions, determine protein structure stability.

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Primary protein structure

The linear sequence of amino acids in a polypeptide chain.

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Secondary protein structure

The localized folding of polypeptide chains into structures like alpha helices and beta sheets.

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Tertiary protein structure

The overall 3D shape of a single polypeptide chain, resulting from interactions among side chains.

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Quaternary protein structure

The arrangement of multiple polypeptide chains into a functional protein complex.

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Hydrophilic vs. Hydrophobic

Hydrophilic amino acids are attracted to water, while hydrophobic ones avoid it.

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Charged vs. Uncharged amino acids

Charged amino acids have a positive or negative charge, while uncharged ones remain neutral.

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Amino group

Part of the amino acid structure containing a nitrogen atom and two hydrogen atoms (–NH2).

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Carboxyl group

Part of the amino acid structure consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydroxyl group (–COOH).

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Study Notes

Introduction to Proteins

  • Macromolecules are considered polymers. A non-polymeric example is a non-polymer chained macromolecule.
  • Proteins have 9 main functions.
  • Draw the common structure of all amino acids, using an "R" to represent the side chain.
  • Identify all 20 amino acid side chains by sight from stick-figure molecules.
  • Determine if an amino acid is polar/nonpolar, charged/uncharged, hydrophilic/hydrophobic.
  • Memorize 3 and 1 letter abbreviations for amino acids.
  • Peptide bonds are between parts of amino acids for the polypeptide backbone.
  • "Residue" is the term for an amino acid when adding to a polypeptide backbone.
  • Folded proteins are usually shown as squiggly lines omitting side chains.
  • Protein folding involves 4 types of side chain-to-side chain bonds of varying strength.
  • Primary, Secondary, Tertiary, and (sometimes) Quaternary structures are involved in protein folding.

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Description

Learn about the structure, function, and folding of proteins. Key topics include amino acids, peptide bonds, and primary, secondary, tertiary, and quaternary structures. Test your knowledge of protein macromolecules and their roles.

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