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How Amino Acids Build Cool Proteins

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Bethan Jones

23/05/2023

Biology

As Level Biology Biochemistry - Protiens

How Amino Acids Build Cool Proteins

A comprehensive guide to protein structure and formation, detailing the complex molecular arrangements of amino acids and their various bonding mechanisms. The text explores how proteins are built from their basic building blocks to complex 3D structures.

  • Structure of amino acids in proteins forms the foundation of protein synthesis, starting with 20 different naturally occurring amino acids
  • Peptide bonds in protein synthesis connect amino acids through condensation reactions to form polypeptide chains
  • Tertiary and quaternary protein structures represent higher-order protein organization, with tertiary involving single chain folding and quaternary involving multiple chains
  • Protein stability depends on various bonds including hydrogen bonds, ionic bonds, and disulfide bridges
  • Denaturation can occur due to temperature and pH changes, affecting protein functionality
...

23/05/2023

96

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

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

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 compactandsolublecompact and soluble or fibrous long,insoluble,andtoughlong, insoluble, and tough.

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

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

Page 7: Protein Denaturation

The final page discusses protein denaturation and its causes.

Definition: Denaturation is the process where protein structure is disrupted by breaking stabilizing bonds.

Highlight: Both high temperature and extreme pH can cause protein denaturation.

Example: Denaturation in globular proteins leads to unfolding and loss of solubility.

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Biology

96

23 May 2023

7 pages

How Amino Acids Build Cool Proteins

user profile picture

Bethan Jones

@bethanjones_jdhy

A comprehensive guide to protein structure and formation, detailing the complex molecular arrangements of amino acids and their various bonding mechanisms. The text explores how proteins are built from their basic building blocks to complex 3D structures.

  • Structure of amino... Show more

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

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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+

Sign up to see the contentIt's free!

Access to all documents

Improve your grades

Join milions of students

By signing up you accept Terms of Service and Privacy Policy

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+

Sign up to see the contentIt's free!

Access to all documents

Improve your grades

Join milions of students

By signing up you accept Terms of Service and Privacy Policy

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 compactandsolublecompact and soluble or fibrous long,insoluble,andtoughlong, insoluble, and tough.

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

Sign up to see the contentIt's free!

Access to all documents

Improve your grades

Join milions of students

By signing up you accept Terms of Service and Privacy Policy

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+

Sign up to see the contentIt's free!

Access to all documents

Improve your grades

Join milions of students

By signing up you accept Terms of Service and Privacy Policy

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+

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Improve your grades

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Page 7: Protein Denaturation

The final page discusses protein denaturation and its causes.

Definition: Denaturation is the process where protein structure is disrupted by breaking stabilizing bonds.

Highlight: Both high temperature and extreme pH can cause protein denaturation.

Example: Denaturation in globular proteins leads to unfolding and loss of solubility.

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

Sign up to see the contentIt's free!

Access to all documents

Improve your grades

Join milions of students

By signing up you accept Terms of Service and Privacy Policy

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 CH3CH3.

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.

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Stefan S

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This app is really great. There are so many study notes and help [...]. My problem subject is French, for example, and the app has so many options for help. Thanks to this app, I have improved my French. I would recommend it to anyone.

Samantha Klich

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Wow, I am really amazed. I just tried the app because I've seen it advertised many times and was absolutely stunned. This app is THE HELP you want for school and above all, it offers so many things, such as workouts and fact sheets, which have been VERY helpful to me personally.

Anna

iOS user

Best app on earth! no words because it’s too good

Thomas R

iOS user

Just amazing. Let's me revise 10x better, this app is a quick 10/10. I highly recommend it to anyone. I can watch and search for notes. I can save them in the subject folder. I can revise it any time when I come back. If you haven't tried this app, you're really missing out.

Basil

Android user

This app has made me feel so much more confident in my exam prep, not only through boosting my own self confidence through the features that allow you to connect with others and feel less alone, but also through the way the app itself is centred around making you feel better. It is easy to navigate, fun to use, and helpful to anyone struggling in absolutely any way.

David K

iOS user

The app's just great! All I have to do is enter the topic in the search bar and I get the response real fast. I don't have to watch 10 YouTube videos to understand something, so I'm saving my time. Highly recommended!

Sudenaz Ocak

Android user

In school I was really bad at maths but thanks to the app, I am doing better now. I am so grateful that you made the app.

Greenlight Bonnie

Android user

very reliable app to help and grow your ideas of Maths, English and other related topics in your works. please use this app if your struggling in areas, this app is key for that. wish I'd of done a review before. and it's also free so don't worry about that.

Rohan U

Android user

I know a lot of apps use fake accounts to boost their reviews but this app deserves it all. Originally I was getting 4 in my English exams and this time I got a grade 7. I didn’t even know about this app three days until the exam and it has helped A LOT. Please actually trust me and use it as I’m sure you too will see developments.

Xander S

iOS user

THE QUIZES AND FLASHCARDS ARE SO USEFUL AND I LOVE THE SCHOOLGPT. IT ALSO IS LITREALLY LIKE CHATGPT BUT SMARTER!! HELPED ME WITH MY MASCARA PROBLEMS TOO!! AS WELL AS MY REAL SUBJECTS ! DUHHH 😍😁😲🤑💗✨🎀😮

Elisha

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This apps acc the goat. I find revision so boring but this app makes it so easy to organize it all and then you can ask the freeeee ai to test yourself so good and you can easily upload your own stuff. highly recommend as someone taking mocks now

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