<h2><em>In general, a scientific law is the description of an observed phenomenon. It doesn't explain why the phenomenon exists or what causes it. The explanation of a phenomenon is called a scientific theory. It is a misconception that theories turn into laws with enough research</em></h2>
Answer:
Well protines come in diffrent shapes, for there diffrent functions. The first level, or primary structure, is the linear sequence of amino acids that creates the peptide chain. In the secondary structure, hydrogen bonding between different amino acids creates a three-dimensional geometry like an alpha helix or pleated sheet. An alpha helix is simply a spiral or coiled molecule, whereas a pleated sheet looks like a ribbon with regular peaks and valleys as part of the fabric. The tertiary structure describes the overall shape of the protein. Most tertiary structures are either globular or fibrous. Generally, nonstructural proteins such as enzymes are globular, which means they look spherical. The enzyme amylase is a good example of a globular protein. Structural proteins are typically long and thin, and hence the name, fibrous. Quaternary structures describe the protein's appearance when a protein is composed of two or more polypeptide chains. Often the polypeptide chains will hydrogen bond with each other in unique patterns to create the desired protein configuration.
some hormones are proteins; and some proteins are involved with digestion, respiration, reproduction, and even normal vision, just to mention a few.
f the three-dimensional structure of the protein is altered because of a change in the structure of the amino acids, the protein becomes denatured and does not perform its function as expected.
Explanation:
Answer:
nucleus-red, membrane-most outer part in of cell in black, centrioles- purple, left the spindle fibers
Answer: This is because water helps in stabilizing the conformation or structure, flexibility of proteins and their movement or motion.
Explanation: Every protein have a particular conformation at which it functions optimally. A protein's conformation is stabilized largely by weak interactions and these weak interactions occur more favorably in aqueous medium. A given polypeptide chain can assume different conformations. The chemical interactions that stabilize the native conformation include include disulfide bonds, hydrogen bonds, hydrophobic and ionic interactions. Hydrogen bonds and hydrophobic interactions are formed in the presence of water, though they are weak interactions but their cumulative effect in a protein is significant. These weak interactions helps to maintain the conformation of proteins and ultimately their function.
