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under web hosting, next to the linux hosting account you want to use, click "manage". In the account dashboard, click cPanel admin. In the cPanel home page, the email section, click "email accounts". In the cPanel email accounts page, next to the email account you want to use, click "manage". Under security, enter a new passwod and then click "update email settings".
Read LessThe four types of chemical bonding is the result of electrostatic attraction between positive and negative charges, or the result of the sharing of electrons. In ionic bonds, positive and negative ions are attracted to one another to form networks of positive and negative charge. In hydrogen bonds, the partial negative charge in one part of a molecule (oxygen, nitrogen, of fluorine) is attracted to the partial positive charge on a hydrogen, and allows the formation of a weak bond. In metalic bonds, positive metal ions are drawn into a shared pool of electrons. Last, covalent bonds result from the direct sharing of valence electrons; since the most stable arrangement is to stick together and share electrons rather than let one atom have all electrons and the other be a charged particle, the covalent bond is quite strong in most cases.
The type of bond that is employed between two particular atoms/molecules depends on their relative electronegativities, meaning their affinity for electrons. If one atom has much higher electron affinity, the bond will be ionic, but if they are similar, bonding will be covalent. Metalic bonds will occur between metal atoms of the same or mixed types of metal. Finally, hydrogen bonding only occurs as the result of partial charges in OH, NH, or FH covalent bonds.
(Not sure what else you might be asking for with "physio".)
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Read LessA protein's 3D structure is largely determined by the primary sequence of the peptide.
First, the primary sequence detirmines the secondary structure of the protein, as groups that are located near one another on the chain interact to form local organized structures (mostly commonly: alpha-helices or beta-pleated sheets).
Furthermore, the primary structure of the peptide determines the tertiary and quaternary structure of the protein, since the R groups of amino acids will interact with each other and the environment. This leads to formation of larger non-localized structures. As a general rule in determining tertiary structure, polar, basic and acidic amino acids will all interact with one another or an aqeuous (water-rich) environment, while non-polar amino acids interact amongst themselves or a non-polar environment-such as a plasma membrane. This means that non-polar amino acids are generally found in the core of the protein where they help to maintain overall structure, while polar/ basic/ acidic amino acids are found either on the protein surface or in an enzymatical active site where they play a greater role interacting with and responding to the environment.
A protein's structure can relate to it's function in many ways, but consider these two points as an example. 1) Some proteins have a completely polar surface, which allows them to be suspended in solution, whereas other proteins have a region that is hydrophobic, as is the case with plasma-membrane associated proteins. 2) Some proteins (enzymes) have an active site where a chemical reaction on a substrate is catalyzed; if misfolded the protein's structure would be wrong and it would not complete the reaction.
Read LessThe most common way of grouping the 20 major amino acids is based on the chemical properties of the side chain (or "R group").
The first group is the non-polar amino acids-Glycine Alanine, Valine, Cysteine, Proline, Leucine, Isoleucine, Methionine, Tryptophan, and Pheylalanine. These amino acids are generally high in hydrocarbon content, which makes them hydrophobic, meaning they are repelled from water. These amino acids will most commonly be found in the core of a protein away from surfaces and typically are a critical component of a protein's overall structure and stability.
The second group, is the basic (or + charge) group, which includes Lysine, Arginine, and Histidine. As suggested by the name, these groups are capable of acting as Bronsted bases, which means they are most stable when they take on a hydrogen and gain a positive charge. These side chains are hydrophillic, which means they will be more likly found on the surface. Due to their ability to take on charge, they are very common components of a protein's active site (to help catalyze a proton transfer for example).
Next, the acidic group (or - charge group) is aspartic acid and glutamic acid. Again, as the name would suggest, they act as bronsted bases and give up their proton to develop a negative charge. They will be found in similar places as the basic group members, though they will typically be involved in different reactions (or may require a combination of acid and base activity).
While the basic and acidic groups are technically also considered polar, "the polar group" includes the amino acids which are polar but do not have acid or base activity. (Note: some people may consider the acid and base groups as a subcategory of the larger polar group.) These amino acids are Serine, Threonin, Tyrosine, Asparagine, and Glutamine. Like the acid and base amino acids, the polar amino acids will most commonly be found at the surfaces of proteins, and may be important components of the active site.
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