main idea : four main types of carbon based molecules are found in living things.

Question

complete the table with functions and examples of each type of carbon based molecule
|molecule type|_functions___|_____examples________|
|___carbohydrate_______|___________|____________|
|___lipid_______|___________|____________|
|___protein_______|___________|____________|
|___nucleaic_acid______|___________|____________|

Answer 1

Here's a completed table outlining the functions and examples of each type of carbon-based molecule found in living things:

| molecule type | functions | examples | |--------------------|--------------------------------------------------|---------------------------------| | carbohydrate | Provide energy, structural support, and storage | Glucose, starch, cellulose, sucrose | | lipid | Store energy, form cell membranes, insulation, and signaling | Fats, oils, phospholipids, steroids | | protein | Catalyze biochemical reactions, provide structure, transport molecules, and regulate processes | Enzymes, antibodies, hemoglobin, collagen | | nucleic acid | Store and transmit genetic information, protein synthesis | DNA, RNA, ATP |

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Answer 2

12. what determines a proteins structure and function?

Answer 3

A protein's structure and function are primarily determined by several key factors:

1. Amino Acid Sequence: The specific sequence of amino acids in a protein, also known as its primary structure, dictates how the protein will fold and ultimately function. The sequence is dictated by the genetic code in DNA.

2. Folding and Primary, Secondary, Tertiary, and Quaternary Structures:

   • Primary Structure: The linear sequence of amino acids.
   • Secondary Structure: Local folding of the amino acid chain into structures such as alpha helices and beta sheets, stabilized by hydrogen bonds.
   • Tertiary Structure: The overall three-dimensional shape of a single polypeptide chain, formed by interactions between the R groups of the amino acids (e.g., hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges).
   • Quaternary Structure: The arrangement of multiple polypeptide chains (subunits) in a protein that is made up of more than one chain. Not all proteins have this structure.

3. Environmental Factors: Conditions such as pH, temperature, and the concentration of ions can affect protein folding and stability. Denaturation can occur if these factors are not within the appropriate range, leading to loss of function.

4. Post-Translational Modifications: After synthesis, proteins can undergo various modifications (e.g., phosphorylation, glycosylation) that can alter their activity, stability, and localization.

5. Interactions with Other Molecules: Proteins often function in complex with other molecules, such as substrates, inhibitors, or cofactors, which can affect their activity and function.

The relationship between a protein's structure and its function is referred to as the "structure-function relationship," which is fundamental to understanding biochemical processes and how proteins perform their roles in the cell.