Amino Acids and Protein Fundamentals

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Questions and Answers

Describe the process by which amino acids are linked together to form a dipeptide, including the specific type of reaction involved.

Amino acids link via a condensation reaction where an amino acid + amino acid forms a dipeptide + water. This process involves the formation of a peptide bond.

Explain what it means for the genetic code to be 'degenerate' and discuss its implications for protein synthesis and mutations.

The genetic code is degenerate because multiple codons can code for a single amino acid. This allows for silent mutations, where a change in the DNA sequence doesn't alter the amino acid sequence of the protein.

Describe the roles of transcription and translation in protein synthesis, clarifying the specific molecules involved in each process.

During transcription, DNA is transcribed into mRNA. During translation, the mRNA is translated into a sequence of amino acids.

How do hydrophobic interactions influence the tertiary structure of a protein, and where do these interactions typically occur within the protein molecule?

Hydrophobic interactions cause nonpolar amino acids to cluster together in the interior of the protein, away from water molecules. This clustering helps to stabilize the protein's three-dimensional shape. Signup and view all the answers

Describe the difference between essential and non-essential amino acids, explaining how each type is obtained by the human body.

Essential amino acids cannot be produced by the body and must be obtained through diet. Non-essential amino acids can be synthesized by the body from other amino acids or by the breakdown of proteins. Signup and view all the answers

Explain how changes in pH can lead to protein denaturation, detailing the specific types of bonds that are affected by these pH variations.

Changes in pH can disrupt ionic bonds and hydrogen bonds within a protein, causing it to unfold and lose its functional shape. Signup and view all the answers

Describe the role R-groups play in determining the chemical diversity of amino acids, and provide two examples of how specific R-group properties affect protein structure or function.

R-groups determine whether an amino acid is polar, nonpolar, acidic, or basic, thus influencing its interactions with other molecules. For example, hydrophobic R-groups cause proteins to fold in ways that exclude water, while charged R-groups can form ionic bonds. Signup and view all the answers

Distinguish between the primary, secondary, and tertiary structures of proteins, explaining what determines each level of structure and how they relate to each other.

The primary structure is the amino acid sequence. Secondary structure involves local folding patterns like alpha helices and beta sheets, stabilized by hydrogen bonds. Tertiary structure is the overall 3D shape of the polypeptide, which stabilized by various chemical bonds and interactions. Signup and view all the answers

What are the roles of hydrogen bonds in the formation of the secondary structure of a protein?

Hydrogen bonds form between the carboxyl group of on amino acid and the amino group of another amino acid helping to stabilize and aid the formation of the secondary structure. Signup and view all the answers

Describe how ionic bonds are formed within proteins, and explain how changes in pH might affect these bonds.

lonic bonding is a type of chemical bond that forms between oppositely charged ions. In proteins, the R-group can undergo binding or dissociation of hydrogen ions, resulting in a positively or negatively charged state. changes in pH can affect these bonds. Signup and view all the answers

What role do disulfide covalent bonds play in stabilizing protein structures, and between which amino acid residues do these bonds typically form?

Disulfide covalent bonds are critical for stabilising the tertiary and quaternary structures of proteins by froming covalent bonds that can help to maintain the protein shape. They form from between pairs of cysteine amino acid residues, which contain sulfur atoms. Signup and view all the answers

Explain the quaternary structure of proteins, including how it is formed and why it is important for protein function. Provide an example of a protein that exhibits quaternary structure.

Quaternary structure refers to the arrangement and interaction of two or more polypeptide chains to form a functional protein. An example is haemoglobin, which consists of four individual polypeptide chains. Signup and view all the answers

Describe the difference between conjugated and non-conjugated proteins, providing an example of each type and explaining the role of the non-protein component in conjugated proteins.

Proteins that consist only of polypeptide subunits are called non-conjugated proteins, like collage. Conjugated proteins have non-protein components like metal ions or carbohydrates, which increase a protein's diversity and functionality. Signup and view all the answers

Globular proteins are soluble in water and play roles in transporting and regulating. Give an example of a globular protein and indicate how hydrophobic interactions contribute to its 3D structure.

Hemoglobin is an example of a globular protein. Hydrophobic interactions can contribute to its 3D structure by clumping nonpolar amino acids together and to minimise contatct with the surrounding water molecules. Signup and view all the answers

Describe the difference between globular and fibrous proteins, focusing on their structure, solubility, and primary functions.

Globular proteins are spherical, soluble, and involved in transport and regulation. Fibrous proteins are long, narrow, insoluble, and provide structural support. Signup and view all the answers

Explain how the structure of insulin (hydrophilic exterior and hydrophobic interior) facilitates its function in the bloodstream.

The hydrophilic exterior allows insulin to interact with water and other hydrophilic molecules in the blood, which is important because insuline needs to travel through bllodstream. Signup and view all the answers

Explain how the sequence of amino acids in a polypeptide chain determines the protein's ultimate three-dimensional structure.

The sequence of amino acids dictates how the chain will fold, driven by interactions between R-groups and the surrounding environment, ultimately determining the protein's structure. Signup and view all the answers

Explain the role of haem in haemoglobin's function, and describe how the interactions between haemoglobin's subunits contribute to its oxygen-carrying capacity.

Haem contains iron, which binds to oxygen. Interactions between subunits allow haemoglobin to undergo conformational changes necessary for its oxygen-carrying function. Signup and view all the answers

How do conditions such as high temperature cause a protein to denature?

High temperature may break down the weak hydrogen bonds. Signup and view all the answers

What is the role of the four substructures of haemoglobin? What could occur, if any of those substructures weren't held together by non covalent bonds?

The four subunits of haemoglobin are held together by non covalent bonds, and the interactions between the subunits allow haemoglobin to undergo conformational changes necessary for its oxygen-carrying function. If the subunits were not held together by non-covalent bonds, they might dissociate or lose the ability to interact correctly, disrupting haemoglobin's ability to bind oxygen efficiently. Signup and view all the answers

Flashcards

Proteins

Complex macromolecules composed of one or more chains of amino acids.

Amino acids

The monomers used to make proteins that are covalently bonded to a central alpha carbon.