Amino Acids and Protein Structure
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Questions and Answers

Which of the following is NOT a function of proteins?

  • Transport
  • Catalysis
  • Storage of genetic information (correct)
  • Signalling

Amino acids consist of a central carbon atom, an amino group, and a carboxylic acid group.

True (A)

Name one structural function of proteins.

Cytoskeleton, muscle, hair or nails.

Proteins are made up of ___________ linked together by peptide bonds.

<p>amino acids</p> Signup and view all the answers

What do enzymes primarily do?

<p>Increase reaction rates by lowering activation energy (B)</p> Signup and view all the answers

Match the following protein functions with their correct descriptions:

<p>Transport = Moving substances across cell membranes Catalysis = Increasing reaction rates Signalling = Regulating cellular responses Structural = Providing shape and support to cells</p> Signup and view all the answers

There are fewer than 300 amino acids found in nature.

<p>False (B)</p> Signup and view all the answers

What is the role of receptors in protein signaling?

<p>To receive signals and play a role in cellular response.</p> Signup and view all the answers

How many amino acids are directly coded by DNA as proteinogenic amino acids?

<p>20 (D)</p> Signup and view all the answers

All amino acids have a three-letter and one-letter abbreviation.

<p>True (A)</p> Signup and view all the answers

What is the conformation of amino acids in protein structure?

<p>L-conformation</p> Signup and view all the answers

The isoelectric point is the point where the net charge of an amino acid is ___ .

<p>0</p> Signup and view all the answers

Match the following amino acids with their characteristics:

<p>Selenocysteine = 21st amino acid in eukaryotes Tyrosine = Amino acid that can be phosphorylated Glutamine = Mutated to Valine in Q6V mutation Amino Acids = Building blocks of proteins</p> Signup and view all the answers

Which of the following amino acids cannot be synthesized in mammals and must be obtained from the diet?

<p>Essential amino acids (A)</p> Signup and view all the answers

Acidic amino acids contain an additional amino group compared to basic amino acids.

<p>False (B)</p> Signup and view all the answers

In an acidic environment, what happens to the concentration of H+ ions?

<p>Increases</p> Signup and view all the answers

What type of bond forms when two cysteine molecules come together?

<p>Disulfide bond (D)</p> Signup and view all the answers

Denaturation alters the primary structure of proteins.

<p>False (B)</p> Signup and view all the answers

What is released during the formation of a peptide bond?

<p>One molecule of water</p> Signup and view all the answers

The secondary structure of proteins is stabilized by ______ bonds.

<p>hydrogen</p> Signup and view all the answers

Which of the following statements about tertiary structure is correct?

<p>It results from interactions of R groups. (C)</p> Signup and view all the answers

What is the term for the process by which proteins regain their natural form after denaturation?

<p>Renaturation</p> Signup and view all the answers

Match the protein structure with its description:

<p>Primary structure = Amino acid sequence Secondary structure = Local hydrogen bonds Tertiary structure = R group interaction Quaternary structure = Multiple polypeptide chains</p> Signup and view all the answers

Hydrophobic amino acids are typically found on the ______ of proteins in aqueous environments.

<p>inside</p> Signup and view all the answers

Flashcards

Protein Functions

Proteins have various roles in living organisms, including catalyzing reactions, transporting substances, signaling, and providing structural support.

Amino Acid Structure

Amino acids have a central carbon atom (alpha carbon) bonded to an amino group, a carboxyl group, and a variable side chain (radical group).

Protein Structure Levels

Proteins have four levels of hierarchical structure: primary, secondary, tertiary, and quaternary.

Protein Structure: Primary

The specific linear sequence of amino acids in a protein.

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Protein Structure: Secondary

The local folding patterns of amino acid chains, like alpha-helices and beta-sheets.

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Protein Structure: Tertiary

The overall 3D shape of a single polypeptide chain.

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Protein Structure: Quaternary

The arrangement of multiple polypeptide chains in a protein complex.

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Protein Denaturation

The loss of a protein's 3D structure and function due to changes in environmental conditions like heat or pH.

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Proteinogenic amino acids

The 20 amino acids directly coded by DNA and used to build proteins.

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Selenocysteine

A 21st amino acid found in eukaryotes, synthesized through special translation mechanisms.

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L-conformation

The specific three-dimensional arrangement of amino acids in proteins.

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Amino acid abbreviations

Each amino acid has a three-letter and one-letter abbreviation for easy notation.

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Amino acid mutations

Changes in the amino acid sequence of a protein, often leading to alterations in its function.

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Essential amino acids

Amino acids that cannot be synthesized by mammals, thus must be obtained from diet.

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Amphoteric molecules

Amino acids can act as both acids (donating H+) and bases (accepting H+).

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Isoelectric point

The pH at which a molecule carries no net electrical charge.

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Peptide Bond Formation

A chemical bond formed between two amino acid molecules. Water is released during the formation.

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Secondary Structure (Proteins)

Local hydrogen bonds between amino acids create folds like alpha-helices and beta-sheets.

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Tertiary Structure (Proteins)

The overall 3D shape of a protein determined by interactions between amino acid side chains (R groups).

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Disulfide Bonds

Strong covalent bonds between sulfur atoms of cysteine amino acids.

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Quaternary Structure (Proteins)

The arrangement of multiple polypeptide chains (subunits) in a protein.

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Denaturation

The process where a protein loses its 3D structure and therefore its function.

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Denaturing agents

Substances (e.g., heat, pH changes, solvents) that cause a protein to lose its 3D structure.

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Renaturation

The process by which a protein regains its 3D structure and function after denaturation, under ideal conditions.

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Study Notes

Amino Acids and Protein Structure

  • Proteins are biomacromolecules composed of amino acids, performing various crucial bodily functions.
  • Learning objectives include listing protein functions, describing amino acid structure, calculating isoelectric points, recognizing protein structures (primary, secondary, tertiary, and quaternary), and explaining protein denaturation.
  • Proteins catalyze metabolic reactions by decreasing activation energy, transporting molecules, acting as hormones for directing metabolism, and giving structural support.
  • DNA contains information for constructing proteins through transcription/translation pathways.

Protein Functions

  • Proteins facilitate various essential tasks in living organisms, including:
  • Catalysis (Enzymes): Increasing metabolic reaction rates by lowering activation energy.
  • Transport: Moving molecules in the circulatory system or between cellular components.
  • Signalling: Directing metabolism within the body via hormones and receptor interactions.
  • Structural Elements: Providing structural support, like cytoskeleton, muscle, hair, and nails.

Protein Structure Summary

  • Proteins have four levels of structure: primary, secondary, tertiary, and quaternary.
  • The primary structure is the linear sequence of amino acid residues.
  • Secondary structure involves local folding patterns like alpha-helices and beta-sheets due to hydrogen bonding.
  • Tertiary structure forms the overall three-dimensional shape, resulting from interactions among amino acid side chains.
  • Quaternary structure emerges when multiple polypeptide chains (subunits) assemble.

Amino Acids

  • More than 300 amino acids exist in nature; however, only 20 are proteinogenic.
  • 20 are directly coded by DNA; others can be incorporated.
  • Amino acids have a central carbon atom (alpha-carbon), an amino group, a carboxyl group, and a variable side chain.
  • Side chains vary in their chemical properties, influencing protein structure and function.
  • Key amino acids include alanine, leucine, phenylalanine, tryptophan, isoleucine, valine, etc.
  • Amino acids can be classified into four groups based on their side chain characteristics:
    • Charged: Basic, acidic.
    • Uncharged Polar: Serine, threonine, etc.
    • Nonpolar: Alanine, valine, etc.

Amino Acids and pH

  • Amino acids are amphoteric molecules, exhibiting both acidic and basic properties.
  • pH affects amino acid structure and charge.
  • Isoelectric point (pI): pH at which the net charge of an amino acid is zero.

Denaturation and Renaturation

  • Denaturation disrupts the secondary, tertiary and quaternary structures of a protein by breaking hydrogen bonds and other interactions, but the primary remains.
  • Renaturation allows a protein to regain its original structure under the required conditions.
  • Factors that cause denaturation include altering pH, temperature, applying certain chemicals (organic solvents).

Essential Amino Acids

  • Some amino acids cannot be synthesized by the human body and must be obtained through diet.
  • These are considered essential amino acids.
  • Examples of essential amino acids are valine, leucine, isoleucine, phenylalanine, threonine, tryptophan, methionine, histidine, and lysine. Other classifications and functions are also relevant within this subject.

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Description

Explore the fascinating world of amino acids and protein structure. This quiz covers protein functions, amino acid properties, and methods of calculating isoelectric points. Delve deeper into the intricacies of protein structures such as primary, secondary, tertiary, and quaternary forms.

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