Answer: The nucleus is a collection of particles called protons, which are positively charged, and neutrons, which are electrically neutral. Protons and neutrons are in turn made up of particles called quarks. The chemical element of an atom is determined by the number of protons, or the atomic number, Z, of the nucleus.
Explanation: big brain
When erosion or deformities occur to a rock layer and then new rock layers are laid on top, the boundary between the deformed layer the new layer is called a(n)B. Unconformity
Receptor receives chemical signals came from the cell's outside environment. It is made up of protein molecule. The correct answer for the question above is letter a. Receptor protein allows one or <span>a few specific molecules to pass across the membrane.</span>
Answer : Option A) He is studying oxygen, which can also be found in proteins.
Explanation : A scientist is examining the role of an element found in fats and carbohydrates of living things. Oxygen is the element which makes up to 65% of human body mass. This is also found in proteins inside the body.
Answer:
The answer is C. its sequence of amino acids.
The protein's shape is influenced by its sequence of amino acids or primary structure.
Explanation:
The primary structure of a protein molecule is dependent on the amino acid chain sequence it has. The amino acid chain's <u>linear</u> structure is composed of <u>covalently bonded</u> amino acids via peptide bonds. This serves as the <u>overall backbone </u>of the protein.
<h3>Additional notes: </h3>
Secondary structure of protein
It defines the 3-dimensional shape of the<u> locally folded polypeptide</u>. They come in two forms, the alpha helices and beta sheets. During the formation of the primary structure, acidic and basic amino residues may cause kinks and turns, re-configuring the 3-D shape of the local polypeptide.
Tertiary structure of protein
This determines the overall 3-dimensional structure of the protein. The structure is due to the <u>linking of the R groups</u> of the related amino acids, <u>hydrophobic bonds</u>, and <u>disulfide bonds</u>. These bonds are <u>highly stable</u> and are not easily changed or destroyed.
Quaternary structure of protein
It is a structure that consists of multiple folded polypeptide chains or subunits. This allows the protein to have m<u>ultiple functions</u>. <u>Non-covalent forces</u> keep these structures together, making it <u>prone to rapid conformational changes.</u>
