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How Amino Acids Build Cool Proteins

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How Amino Acids Build Cool Proteins
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Bethan Jones

@bethanjones_jdhy

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12 Followers

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Proteins are complex biomolecules essential for life, composed of amino acids linked by peptide bonds in protein synthesis. They perform various crucial functions in organisms, from structural support to enzymatic catalysis. The structure of amino acids in proteins determines their unique properties and functions.

  • Proteins are polymers of amino acids with diverse roles (e.g., hemoglobin, enzymes, antibodies)
  • Amino acids have a common structure with variable R groups
  • Protein structure is hierarchical: primary, secondary, tertiary, and quaternary
  • Various bonds and interactions maintain protein structure
  • Protein denaturation occurs when these structures are disrupted

23/05/2023

92

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

Amino Acid Types and Peptide Bond Formation

Amino acids are classified based on their R groups, which can be simple, hydroxyl, sulphur-containing, cyclic, basic, acidic, or ringed. This diversity allows for the creation of proteins with a wide range of properties and functions.

Vocabulary: Peptide bond - A covalent bond formed between the carboxyl group of one amino acid and the amino group of another, resulting in the release of a water molecule.

The formation of polypeptides occurs through condensation reactions, where amino acids join together, releasing water molecules in the process. This reaction can continue, forming longer chains that eventually become proteins.

Example: Lysine, an amino acid with a basic R group, has a side chain ending in an NH3+ group, which contributes to its ability to form ionic bonds within proteins.

Highlight: The sequence and types of amino acids in a polypeptide chain determine the protein's primary structure, which is crucial for its final three-dimensional shape and function.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

Amino Acid Structure and Protein Formation

The foundation of proteins lies in the structure of amino acids. Each amino acid consists of a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable R group. This R group determines the specific properties of each amino acid.

Vocabulary: Amphoteric - Capable of resisting changes in pH, a characteristic of proteins due to their amino acid composition.

Proteins are formed through condensation reactions between amino acids, creating peptide bonds. This process results in the formation of polypeptides, which can further combine to create complex protein structures.

Example: Glycine, the simplest amino acid, has a hydrogen atom as its R group, while alanine has a methyl group (CH3).

Highlight: There are 20 different naturally occurring amino acids found in proteins, each with a unique R group that contributes to the protein's overall structure and function.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

Protein Structure Levels

Proteins exhibit four levels of structure, each building upon the previous:

  1. Primary Structure: The sequence of amino acids in the polypeptide chain.
  2. Secondary Structure: Regular patterns formed by hydrogen bonding between amino acids, such as alpha helices and beta sheets.
  3. Tertiary and quaternary protein structures: The three-dimensional folding of the entire polypeptide chain and the arrangement of multiple polypeptide subunits, respectively.

Definition: Protein sequencing - The process of determining the primary structure of a protein by identifying the order of its amino acids.

Example: The alpha helix is a common secondary structure where the polypeptide chain twists into a regular spiral, stabilized by hydrogen bonds between amino acids.

Highlight: The tertiary structure is responsible for a protein's unique properties and functions, held together by various bonds between the R groups of amino acids.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

Protein Structure Comparison

Globular and fibrous proteins have distinct structural characteristics:

Globular Proteins:

  • Compact, spherical shape
  • Often soluble in water
  • Examples include enzymes and hemoglobin

Fibrous Proteins:

  • Long, parallel chains with cross-linkages
  • Insoluble and tough
  • Relatively unaffected by temperature or pH changes
  • Examples include collagen and keratin

Example: Collagen, a fibrous protein, consists of three identical polypeptide chains, while hemoglobin, a globular protein, has four different polypeptide subunits.

Highlight: The highest level of structure in collagen is secondary, whereas hemoglobin exhibits quaternary structure.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

Bonds in Protein Structure

Various types of bonds and interactions contribute to maintaining protein structure:

  1. Hydrogen bonds: Weak interactions between partially charged atoms.
  2. Ionic bonds: Strong interactions between oppositely charged groups.
  3. Disulphide bonds: Strong covalent bonds between cysteine amino acids.
  4. Hydrophobic interactions: Attractions between non-polar R groups.
  5. Van der Waals forces: Weak attractions between atoms in close proximity.

Example: Hemoglobin, the oxygen-carrying protein in red blood cells, exhibits quaternary structure with four polypeptide chains arranged in a tetrahedral shape.

Highlight: The final three-dimensional shape of a protein can be classified as globular (compact and soluble) or fibrous (long, insoluble, and tough).

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

Protein Denaturation

Denaturation is the process by which a protein's structure is altered, often resulting in loss of function:

  • High temperatures can break hydrogen bonds, causing globular proteins to unfold and become insoluble.
  • Extreme pH levels can disrupt ionic bonds by altering the charges on R groups.

Definition: Denaturation - The alteration of a protein's structure, often leading to loss of its biological function.

Highlight: Protein structure relies heavily on the strong ionic bonds between positively and negatively charged R groups found on amino acids.

Understanding protein structure and denaturation is crucial for many biological processes and has important implications in fields such as medicine and biotechnology.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

View

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How Amino Acids Build Cool Proteins

user profile picture

Bethan Jones

@bethanjones_jdhy

·

12 Followers

Follow

Proteins are complex biomolecules essential for life, composed of amino acids linked by peptide bonds in protein synthesis. They perform various crucial functions in organisms, from structural support to enzymatic catalysis. The structure of amino acids in proteins determines their unique properties and functions.

  • Proteins are polymers of amino acids with diverse roles (e.g., hemoglobin, enzymes, antibodies)
  • Amino acids have a common structure with variable R groups
  • Protein structure is hierarchical: primary, secondary, tertiary, and quaternary
  • Various bonds and interactions maintain protein structure
  • Protein denaturation occurs when these structures are disrupted

23/05/2023

92

 

12

 

Biology

6

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Amino Acid Types and Peptide Bond Formation

Amino acids are classified based on their R groups, which can be simple, hydroxyl, sulphur-containing, cyclic, basic, acidic, or ringed. This diversity allows for the creation of proteins with a wide range of properties and functions.

Vocabulary: Peptide bond - A covalent bond formed between the carboxyl group of one amino acid and the amino group of another, resulting in the release of a water molecule.

The formation of polypeptides occurs through condensation reactions, where amino acids join together, releasing water molecules in the process. This reaction can continue, forming longer chains that eventually become proteins.

Example: Lysine, an amino acid with a basic R group, has a side chain ending in an NH3+ group, which contributes to its ability to form ionic bonds within proteins.

Highlight: The sequence and types of amino acids in a polypeptide chain determine the protein's primary structure, which is crucial for its final three-dimensional shape and function.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Amino Acid Structure and Protein Formation

The foundation of proteins lies in the structure of amino acids. Each amino acid consists of a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable R group. This R group determines the specific properties of each amino acid.

Vocabulary: Amphoteric - Capable of resisting changes in pH, a characteristic of proteins due to their amino acid composition.

Proteins are formed through condensation reactions between amino acids, creating peptide bonds. This process results in the formation of polypeptides, which can further combine to create complex protein structures.

Example: Glycine, the simplest amino acid, has a hydrogen atom as its R group, while alanine has a methyl group (CH3).

Highlight: There are 20 different naturally occurring amino acids found in proteins, each with a unique R group that contributes to the protein's overall structure and function.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Protein Structure Levels

Proteins exhibit four levels of structure, each building upon the previous:

  1. Primary Structure: The sequence of amino acids in the polypeptide chain.
  2. Secondary Structure: Regular patterns formed by hydrogen bonding between amino acids, such as alpha helices and beta sheets.
  3. Tertiary and quaternary protein structures: The three-dimensional folding of the entire polypeptide chain and the arrangement of multiple polypeptide subunits, respectively.

Definition: Protein sequencing - The process of determining the primary structure of a protein by identifying the order of its amino acids.

Example: The alpha helix is a common secondary structure where the polypeptide chain twists into a regular spiral, stabilized by hydrogen bonds between amino acids.

Highlight: The tertiary structure is responsible for a protein's unique properties and functions, held together by various bonds between the R groups of amino acids.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Protein Structure Comparison

Globular and fibrous proteins have distinct structural characteristics:

Globular Proteins:

  • Compact, spherical shape
  • Often soluble in water
  • Examples include enzymes and hemoglobin

Fibrous Proteins:

  • Long, parallel chains with cross-linkages
  • Insoluble and tough
  • Relatively unaffected by temperature or pH changes
  • Examples include collagen and keratin

Example: Collagen, a fibrous protein, consists of three identical polypeptide chains, while hemoglobin, a globular protein, has four different polypeptide subunits.

Highlight: The highest level of structure in collagen is secondary, whereas hemoglobin exhibits quaternary structure.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Bonds in Protein Structure

Various types of bonds and interactions contribute to maintaining protein structure:

  1. Hydrogen bonds: Weak interactions between partially charged atoms.
  2. Ionic bonds: Strong interactions between oppositely charged groups.
  3. Disulphide bonds: Strong covalent bonds between cysteine amino acids.
  4. Hydrophobic interactions: Attractions between non-polar R groups.
  5. Van der Waals forces: Weak attractions between atoms in close proximity.

Example: Hemoglobin, the oxygen-carrying protein in red blood cells, exhibits quaternary structure with four polypeptide chains arranged in a tetrahedral shape.

Highlight: The final three-dimensional shape of a protein can be classified as globular (compact and soluble) or fibrous (long, insoluble, and tough).

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Protein Denaturation

Denaturation is the process by which a protein's structure is altered, often resulting in loss of function:

  • High temperatures can break hydrogen bonds, causing globular proteins to unfold and become insoluble.
  • Extreme pH levels can disrupt ionic bonds by altering the charges on R groups.

Definition: Denaturation - The alteration of a protein's structure, often leading to loss of its biological function.

Highlight: Protein structure relies heavily on the strong ionic bonds between positively and negatively charged R groups found on amino acids.

Understanding protein structure and denaturation is crucial for many biological processes and has important implications in fields such as medicine and biotechnology.

Proteins
Proteins are polymers whose molecules are made from many amino acids.
examples = haemoglobin, enzymes, antibodies, collegen (bone+

Can't find what you're looking for? Explore other subjects.

Knowunity is the #1 education app in five European countries

Knowunity has been named a featured story on Apple and has regularly topped the app store charts in the education category in Germany, Italy, Poland, Switzerland, and the United Kingdom. Join Knowunity today and help millions of students around the world.

Ranked #1 Education App

Download in

Google Play

Download in

App Store

Knowunity is the #1 education app in five European countries

4.9+

Average app rating

13 M

Pupils love Knowunity

#1

In education app charts in 12 countries

950 K+

Students have uploaded notes

Still not convinced? See what other students are saying...

iOS User

I love this app so much, I also use it daily. I recommend Knowunity to everyone!!! I went from a D to an A with it :D

Philip, iOS User

The app is very simple and well designed. So far I have always found everything I was looking for :D

Lena, iOS user

I love this app ❤️ I actually use it every time I study.