Proteins & Enzymes Overview
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Questions and Answers

What is the name of the sweetner that is about 200 times sweeter than common table sugar (sucrose)?

Aspartame

What are the two main secondary protein structures?

Alpha helix and beta pleated sheet

Define a primary structure, in terms of protein.

The primary structure of a protein consists of a sequence of amino acids linked together by peptide bonds and includes any disulfide bonds.

What are the 4 factors that are responsible for tertiary structures of proteins?

<p>Disulfide linkages, hydrogen bonding, electrostatic interactions, and hydrophobic interactions.</p> Signup and view all the answers

What is the protein that is a good example of a protein with Quaternary structure?

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

What is the term used for the unfolding of the protein molecule?

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

Higher temperatures promote denaturation.

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

What are the properties of amino acids that make them good emulsifiers?

<p>They are amphiphilic because they contain both hydrophobic and hydrophilic groups.</p> Signup and view all the answers

What are the 4 factors that affect protein-based emulsions?

<p>Solubility of protein, distribution of hydrophobic vs. hydrophilic amino acids, shape of protein, and flexibility of protein.</p> Signup and view all the answers

What is the process called when the protein is broken down into its individual constituent amino acids?

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

Flashcards

Tertiary structure

The overall three-dimensional arrangement of all atoms in a protein.

Primary structure

The specific sequence of amino acids in a protein.

Secondary structure

The local folding patterns of the polypeptide chain like alpha-helix and beta-sheet.

Denaturation

Breakdown and unfolding of a protein's structure, disrupting its function.

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Alpha-helix

A type of secondary structure characterized by a helical arrangement of amino acids.

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Beta-sheet

A type of secondary structure characterized by flat, extended regions of amino acids arranged in a sheet-like structure.

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Disulfide bond

A chemical bond formed between two cysteine amino acid residues, stabilizing protein tertiary structure.

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Hydrogen bond

Weak interactions involving the sharing of a hydrogen atom between two electronegative atoms.

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Electrostatic interactions

Interactions between oppositely charged groups of amino acids within a protein.

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Hydrophobic interactions

Interactions between nonpolar side chains of amino acids, driven by their aversion to water.

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Ion exchange chromatography

A method used to separate amino acids based on their charge properties.

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High-Performance Liquid Chromatography (HPLC)

A type of chromatography that separates molecules based on their affinity for a stationary phase.

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Edman Degradation

A method for determining the amino acid sequence of a protein.

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TLCMS

A method for determining the amino acid composition of a protein.

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Chaperone protein

A substance that can bind to and stabilize the structure of a protein.

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Protease

A protein that can break down other proteins into smaller peptides.

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Glycation

The process of modifying a protein by attaching a sugar molecule to it.

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Hydration

The ability of a protein to attract and hold water molecules.

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Gelation

The ability of a protein to form a stable, rigid structure.

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Emulsification

The ability of a protein to decrease surface tension between two liquids, allowing them to mix.

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Foaming

The ability of a protein to trap gas bubbles, creating foam.

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Gelation

The ability of a protein to form a stable, rigid structure.

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Chaperone protein

A substance that can bind to and stabilize the structure of a protein.

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Solubility

The property of a protein that allows it to be dissolved in a solvent.

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Protein content

A measure of the concentration of a protein in a solution.

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Glycation

The process of modifying a protein by attaching a sugar molecule.

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Chaperone protein

A substance that can bind to and stabilize the structure of a protein.

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Protein hydrolysis

The process of breaking down a protein into smaller peptides.

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Hydration

The ability of a protein to attract and hold water molecules.

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Gluten

A type of protein found in wheat that gives dough its elasticity.

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Dispersed system

A mixture of two or more substances that are not dissolved in each other.

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Solubility

The property of a protein to be dissolved in a solvent.

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Hydration

The ability of a protein to attract and hold water molecules.

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Chaperone protein

A substance that can bind to and stabilize the structure of a protein.

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Study Notes

Proteins & Enzymes

  • Proteins are the workhorses of biological systems.
  • They play a crucial role in building and maintaining living cells.
  • Proteins are polymers of amino acids.
  • Amino acids are the basic building blocks.
  • Peptides are short polymers of amino acids (up to 40).
  • Proteins have four levels of structure: primary, secondary, tertiary, and quaternary.
  • Primary structure is the sequence of amino acids in a polypeptide chain.
  • Secondary structure includes alpha-helices and beta-pleated sheets, formed by hydrogen bonds.
  • Tertiary structure is the three-dimensional arrangement of the polypeptide chain.
  • Quaternary structure describes the arrangement of multiple polypeptide chains.
  • Proteins perform various roles, including enzymes, hormones, storage, transport, structural, protective, contractile, and toxic proteins.
  • Enzymes are biological catalysts, speeding up reactions.
  • They decrease the activation energy needed for reactions.
  • Enzymes are highly specific to the type of reaction they catalyze and the substrates they act on.
  • The active site is the region on the enzyme where the substrate binds and reaction occurs.

Amino Acids

  • Around 500 amino acids are known.
  • Only 20 are used to form proteins in eukaryotes (22 in total)
  • Selenocysteine and pyrrolysine are incorporated into proteins via special mechanisms.
  • 11 amino acids can be produced in the body, the other 9 are essential amino acids.
  • Amino acids have an amino group, a carboxyl group, a hydrogen atom, and a variable side chain.
  • Amino acids can be classified based on their side chain properties: polar, nonpolar, acidic, or basic.

Protein Structure and Function

  • Proteins are polymers of 2-amino-carboxylic acids.
  • The α-carbon atom in amino acids is a chiral center.
  • All amino acids in biological systems are L-enantiomers.
  • Amino acids have an amino end (N-terminus) and a carboxyl end (C-terminus).
  • The primary structure is determined by the sequence of amino acids linked by peptide bonds.
  • The sequence dictates the protein’s properties and function.
  • Alterations in the amino acid sequence can lead to a loss of protein function.

Protein Sequence Determination

  • Determining the amino acid sequence is done via Edman degradation (often on smaller proteins).
  • Automated machines exist for this; often starting by determining N-terminal amino acid.
  • Mass spectrometry can also be used to determine protein sequence.

Protein Classification

  • Classifying proteins based on structure, roles, and other properties.
  • Globular (spherical) versus fibrous (linear) proteins based on shape.
  • Solubility is a key factor, depending on amino acid makeup and secondary/tertiary structure.

Protein Denaturation

  • Denaturation is the loss of a protein's native, functional three-dimensional structure.
  • This happens due to various factors like temperature (heat), solvents, pH, and chemicals.
  • These factors disrupt the bonds and interactions holding the protein in its native conformation.
  • Denatured proteins often become insoluble and lose their biological activity.

Functional Properties of Proteins

  • Proteins influence structure, taste, texture, aroma, and viscosity in foods.
  • The ability to bind water is crucial for various food processes.
  • Proteins affect dough formation, and various other food properties.
  • Several aspects influence functional protein properties like shape/structure, hydrophobicity, type of amino acid, flexibility, etc.

Protein Interactions and Phenomena Affected in Food Systems

  • Proteins interaction with components such as water, ions and other macromolecules.
  • The capacity to bind water
  • These interactions affect various food properties, including wettability, swelling, water sorption, water retention, viscosity, emulsion formation, foaming, and gelation.

Enzyme Activity and Classification

  • Enzymes are biological catalysts.
  • They speed up reactions by lowering the activation energy.
  • Enzymes are highly specific for their substrates and the reactions they catalyze.
  • Different classifications of enzymes exist, based on the reaction type.

Enzyme Deactivation

  • High temperature processing can be used to deactivate enzymes to prevent unwanted reactions during food processing.

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Proteins and Enzymes PDF

Description

This quiz covers the essential aspects of proteins and enzymes, including their structures, functions, and importance in biological systems. Learn about the four levels of protein structure and the role enzymes play as biological catalysts. Test your knowledge about the building blocks of proteins and their diverse functionalities.

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