How does protein folding happen?

How does protein folding happen? *Note: This article is from the book The Darwin Black Box: The Biochemistry Challenge of Evolution. The protein usually contains between 50 and 3000 amino acid drunks, and the initial sequence of amino acids in the protein is called the primary structure, and the completed protein will still have free ends of the amino group usually denoted by the terminal end (N) and a free carboxylic group called the terminal end (C). The amino sequence is usually written starting from the terminal (N) to the terminal (C). In an interesting process, almost all proteins are involved in the formation of precise and distinct structures that can be completely different between different proteins, and this happens automatically as a result of different interactions, such as attracting positively charged and negatively charged chains, or combining hydrophobic side chains to separate them, or excluding large side chains from narrow spaces and so on. When proteins are involved, they don't suddenly pile together, as a protein does in your hand when it piles up, but there are rules that regulate this action. Before a protein is involved, the atoms of its polar backbone -- the oxygen, nitrogen, and hydrogen atoms in each peptide bond -- will form what's called a hydrogen bond with water molecules, and the hydrogen bond is established when the charged peptide oxygen or nitrogen is partially bonded to the hydrogen atoms in the water. There are two ways in which a protein can solve a problem. First, parts of the protein can form a structure called an alpha helix, in which case the backbone of the protein will wrap itself, and this bypass geometry makes the oxygen atoms in the peptide groups directly correspond to the hydrogen atoms of the peptide groups in the four amino strands along the chain forming hydrogen bonds, and the next hydrogen bond is usually a solution with the four strands. Another structure that allows the regulation of hydrogen bonds between peptide atoms is called the peptide plate or beta fold. In this structure, the backbone of the protein is like the bent plate, up and down, and the peptide atoms attach to the surface of the slope according to the direction of the chain, and then the chain rolls back. Snails and plates are defined as the secondary structure of proteins. A typical protein has 40 to 50 percent of the amino residues contained in those snails or plates. The remaining acids will either enter between the secondary structure sections or form irregular structures. The helixes and plates are stacked against each other to form, in most cases, a spherical protein, the way the secondary structure elements are stacked is called the tertiary structure of the protein, and the driving force of the helix and plate stacking comes from the oily nature of many amino acids. As the oils separate from the water by a distinct layer, the hydrophobic chains combine to form a water-free zone within the protein. However, remember that some protein side chains are either polarized or charged and prefer to stay in the water, hence the information that leads a particular protein to fold into a specific structure, as the pattern of polarized or oily side chains in the amino acid sequence dictates the need for the protein chain to involve most of the protein chains. Another factor that also contributes to protein folding is that in all embedded proteins, some of the polar chains are embedded in a hydrophobic structure. If the polar atoms are unable to find a partner with which to form hydrogen bonds, then the protein balance is disturbed, but in most proteins, about 90% of the embedded polar chains form hydrogen bonds with the atoms of the protein structure or with other side chains in a pattern called "connect as much as you can". Many peptides adhere to each other in high quality to form a structure that acts as a complete unit, and in such cases, it is customary to refer to the associated peptide chains as a single protein composed of many subunits. For example, hemoglobin (an oxygen-carrying protein) is made up of four peptides, and the protein assembled from those chains is capable of functioning as an oxygen transporter. - Dr. Michael Behe. — Source: Brahin Center website - Published on 2018-10-11 (archived at the Internet Archive) https://braheen.com/articles/evolution-design/كيف-يحدث-طي-البروتينات