Amino Acids and Protein Structure Quiz
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Questions and Answers

Which of the following is NOT a function of proteins?

  • Catalysis
  • Transport
  • Signalling
  • Energy storage (correct)

Amino acids consist of a central carbon atom, an amino group, and only one functional group.

False (B)

What are the four structures in proteins that can be recognized?

Primary, secondary, tertiary, and quaternary structures

Proteins that increase the reaction rate of metabolic reactions are known as ______.

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

Match the following protein functions with their descriptions:

<p>Catalysis = Increases reaction rates Transport = Moves substances in the body Signalling = Regulates metabolic processes Structural Elements = Provides support and shape</p> Signup and view all the answers

Which part of the amino acid structure varies among different amino acids?

<p>Radical group (side chain) (C)</p> Signup and view all the answers

There are fewer than 300 amino acids that can be found in nature.

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

What is the primary role of hemoglobin in the body?

<p>Transporting oxygen</p> Signup and view all the answers

What type of bond is formed between two cysteine amino acids?

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

Denaturation results in a change in the primary structure of proteins.

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

What is the term for the loss of biological activity in proteins without a change in primary structure?

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

The ___ structure of proteins involves local hydrogen bonds between amino acids.

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

How many amino acids are primarily coded by DNA for protein synthesis?

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

Match the types of protein structure to their definitions:

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

Selenocysteine is considered the 21st amino acid in eukaryotes.

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

Which of the following processes involves gaining natural form after denaturation?

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

What conformation are amino acids in protein structures always found?

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

Hydrophobic amino acids are found on the surface of proteins in aqueous media.

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

Essential amino acids cannot be synthesized in __________ and must be obtained from the diet.

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

Match the following terms with their descriptions:

<p>Amphoteric = Can act as both an acid and a base Isoelectric point = The point where net charge is zero Acidic amino acids = Contain an additional carboxyl group Basic amino acids = Contain an additional amino group</p> Signup and view all the answers

During peptide bond formation, one molecule of ___ is released.

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

Which of the following statements is true regarding amino acids?

<p>All amino acids have a one-letter and three-letter abbreviation. (C)</p> Signup and view all the answers

Asidic environment corresponds to a high pH.

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

What happens to an amino acid when a phosphate group is added?

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

Flashcards

Protein Functions

Proteins play vital roles in biological processes, including catalysis (enzyme function), transport, signaling, and structural support.

Amino Acid Structure

Amino acids have a central carbon atom (alpha carbon) bonded to an amino group (-NH2), a carboxyl group (-COOH), and a side chain (radical group).

Protein Catalysis

Proteins act as enzymes to speed up chemical reactions in the body by lowering the activation energy.

Protein Transport

Proteins facilitate the movement of molecules throughout the body, like carrying oxygen or nutrients.

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Protein Signaling

Proteins act as hormones and receptors, regulating bodily functions and responses to signals.

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Protein Structure: Primary

The primary structure of a protein is the linear sequence of amino acids.

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Protein Structure: Secondary

Secondary protein structure refers to the folding patterns of the amino acid chain resulting from hydrogen bonds.

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Protein Structure: Amino Acids

Amino acids are the building blocks of proteins.

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Peptide Bond Formation

The process of joining two amino acids together, releasing one water molecule.

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Secondary Structure

Local, 3D arrangements of amino acids within a protein chain, stabilized by hydrogen bonds. Common structures include α-helices and β-sheets.

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Tertiary Structure

The overall 3D shape of a single protein chain, arising from interactions between amino acid side chains.

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Hydrophobic Interactions

A driving force in tertiary structure where non-polar amino acids cluster together to avoid water.

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Disulfide Bonds

Strong covalent bonds between two cysteine residues, important for maintaining protein shape.

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Quaternary Structure

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

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Denaturation

The process of disrupting a protein's shape, leading to loss of biological function.

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Renaturation

The process of restoring a denatured protein to its native, functional state.

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Proteinogenic amino acids

The 20 amino acids directly coded for by DNA's genetic code, found as constituents of proteins.

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Selenocysteine

A 21st amino acid used in protein synthesis, found in eukaryotes.

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L- amino acids in protein

Proteins always contain amino acids in L-conformation.

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Essential amino acids

Amino acids that mammals cannot produce and must obtain from their diet.

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Amino acid abbreviation

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

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Amino Acids and pH

Amino acids are amphoteric, acting as both acids and bases, in response to changes in pH, their net charge changes as well.

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Isoelectric point

The pH at which an amino acid has a net charge of zero.

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Primary Structure of Protein

The linear sequence of amino acids in a polypeptide chain.

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Study Notes

Amino Acids and Protein Structure

  • Proteins are biomacromolecules composed of amino acids.
  • Proteins have diverse functions, including catalysis, transport, signaling, and structural support.
  • Learning objectives include listing protein functions, describing amino acid structure, calculating isoelectric points, and recognizing protein structures.

Learning Objectives

  • List the functions of proteins.
  • Describe the structure of amino acids.
  • Calculate isoelectric points.
  • Describe the bonds forming proteins.
  • Recognize primary, secondary, tertiary, and quaternary structures in proteins.
  • Explain protein denaturation.

Proteins

  • Proteins are responsible for various important duties.
  • They are biomacromolecules made of amino acids.

DNA, RNA, and Protein

  • DNA → RNA → Protein
  • DNA replication, transcription, and translation are crucial processes.

Protein Functions - Catalysis

  • Enzymes increase reaction rates by lowering activation energy.
  • Maltose to Glucose in 1 sec, normally it's 300 years.

Protein Functions - Transport

  • Proteins transport substances in the circulatory system and between cellular compartments.
  • Examples include hemoglobin and lipoproteins.

Protein Functions - Signaling

  • Proteins act as hormones, directing and regulating metabolism.
  • Receptors receive signals and play vital roles in cellular responses.

Protein Functions - Structural Elements

  • Proteins form cytoskeletal elements, muscles, hair, and nails, providing essential structural support.
  • Some proteins are solely structural.

Protein Structure

  • RNA creates 3D structures.

Amino Acids

  • Amino acids have different shapes.
  • There are more than 300 amino acids in nature but only 20 are constituents of proteins.
  • Some amino acids have special roles, like selenocysteine in eukaryotes.
  • Amino acids have a central carbon atom, a carboxyl group, an amino group, and a variable side chain (radical). This side-chain gives it various properties.
  • They can be positive, negative, or neutral. The side chains' properties determine how the amino acid interacts with water and other molecules.

Amino Acids - 21st Amino Acid

  • In eukaryotes, selenocysteine (21st) is also used.

L- and D- Isomers

  • Amino acids in proteins are L-isomers.
  • They exist as mirror-image isomers.

Amino Acids - Acidic Side Chains

  • Aspartic and glutamic acids.

Amino Acids - Basic Side Chains

  • Lysine, arginine, and histidine.

Amino Acids - Polar Uncharged Side Chains

  • Serine, threonine, asparagine, glutamine, cysteine, glycine, proline.

Amino Acids - Hydrophobic Side Chains

  • Alanine, isoleucine, leucine, methionine, phenylalanine, tryptophan, tyrosine, valine.

Amino Acids and pH

  • Amino acids are amphoteric molecules.
  • They have both acidic and basic properties.
  • The net charge of an amino acid depends on pH.
  • Isoelectric point (pI) is the pH where the net charge is zero.

Primary Structure

  • Consists of the amino acid sequence arranged in a linear chain.
  • Peptide bonds connect amino acids.

Secondary Structure

  • Local hydrogen bonds between amino acids result in structures like alpha-helices and beta-sheets.

Tertiary Structure

  • Interactions between amino acids form a compact 3D structure with interactions from hydrophobic/hydrophilic amino acids.
  • Numerous interactions maintain the shape: disulfide bridges, hydrogen bonds, ionic bonds, and hydrophobic interactions.

Quaternary Structure

  • Multiple polypeptide chains form a larger structure, such as in hemoglobin. Also determined by interactions of R groups.

Denaturation

  • Denaturation is the loss of protein's 3D structure. This leads to a loss of biological activity.
  • Caused by factors such as temperature, pH, organic solvents, heavy metals, and detergents.

Renaturation

  • Protein's regaining its natural form after denaturation is called renaturation.
  • It depends on specific conditions.

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Description

Test your knowledge on amino acids and protein structure. This quiz covers protein functions, amino acid structure, isoelectric points, and the different levels of protein structure. Dive into the essential roles proteins play in biological systems and understand their formation processes.

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