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They have varying chemical compositions, which allows them to code for different proteins.
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Describe a generalised structure of amino acids?
Amino acids have a generalised structure consisting of an amino group (-NH2), a carboxyl group (-COOH), and a side chain represented by the letter "R". The side chain can vary among different amino acids, giving them distinct chemical properties. The central carbon atom (alpha carbon) connects the amino group, carboxyl group, and the side chain, forming the backbone of the amino acid.
Which three components are common to all amino acids?
The 20 amino acids vary in structure by the R-group, otherwise all amino acids are the same in structure. All amino acids have a carboxyl group, an amino group, an R-group, and a hydrogen which are all bonded to a central carbon. It is the R-groups that make the amino acids react in different ways and alter the structure of the protein.
Can proteins form polymers?
Yes, proteins are formed from amino acid monomers. The OH group on one end of the amino acid bonds with the hydrogen group on the other end to form a water molecule. Then the peptide bond forms (carbon-nitrogen-carbon)
What determines the identity of an amino acid in a proteins?
Amino acids play central roles both as building blocks of proteins and as intermediates in metabolism. The 20 amino acids that are found within proteins convey a vast array of chemical versatility. The precise amino acid content, and the sequence of those amino acids, of a specific protein, is determined by the sequence of the bases in the gene that encodes that protein. The chemical properties of the amino acids of proteins determine the biological activity of the protein. Proteins not only catalyze all (or most) of the reactions in living cells, they control virtually all cellular process. In addition, proteins contain within their amino acid sequences the necessary information to determine how that protein will fold into a three dimensional structure, and the stability of the resulting structure. The field of protein folding and stability has been a critically important area of research for years, and remains today one of the great unsolved mysteries. It is, however, being actively investigated, and progress is being made every day.As we learn about amino acids, it is important to keep in mind that one of the more important reasons to understand amino acid structure and properties is to be able to understand protein structure and properties. We will see that the vastly complex characteristics of even a small, relatively simple, protein are a composite of the properties of the amino acids which comprise the protein.Essential amino acidsHumans can produce 10 of the 20 amino acids. The others must be supplied in the food. Failure to obtain enough of even 1 of the 10 essential amino acids, those that we cannot make, results in degradation of the body's proteins-muscle and so forth-to obtain the one amino acid that is needed. Unlike fat and starch, the human body does not store excess amino acids for later use-the amino acids must be in the food every day.The 10 amino acids that we can produce are alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine. Tyrosine is produced from phenylalanine, so if the diet is deficient in phenylalanine, tyrosine will be required as well. The essential amino acids are arginine (required for the young, but not for adults), histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These amino acids are required in the diet. Plants, of course, must be able to make all the amino acids. Humans, on the other hand, do not have all the the enzymes required for the biosynthesis of all of the amino acids.Why learn these structures and properties?It is critical that all students of the life sciences know well the structure and chemistry of the amino acids and other building blocks of biological molecules. Otherwise, it is impossible to think or talk sensibly about proteins and enzymes, or the nucleic acids.
How does protein structure affect protein function?
The primary structure is simply a long chain of peptides (polypeptide chain). The peptide monomers are like letters in a long, long word (the polypeptide). The word, a product of the primary structure and the peptide bonding sequence means something - whether it be, "I'm a transport protein." or "I'm an enzyme!". So, the primary structure definitely dictates the function of a protein by the sequence of amino acids it has. The primary structure's sequence of amino acids also dictates how the polypeptide will form (its structure). The R-group on the amino acids, which varies, will cause an amino acid to be positive, negative, polar, or nonpolar. This will cause the peptide chain, after these amino acids have been put together through dehydration reactions, to attract/form bonds with each other differently, leading to specific structures based off of the primary structure of a protein. These bonds vary between hydrophobic interactions, van der Waals attractions, hydrogen bonds, disulfide bridges, and a couple of other bonds. These new bonds and formations result in the secondary and tertiary levels of structure
What are the component of amino acid?
The 20 amino acids vary in structure by the R-group, otherwise all amino acids are the same in structure. All amino acids have a carboxyl group, an amino group, an R-group, and a hydrogen which are all bonded to a central carbon. It is the R-groups that make the amino acids react in different ways and alter the structure of the protein.
Describe a generalised structure of amino acids?
Amino acids have a generalised structure consisting of an amino group (-NH2), a carboxyl group (-COOH), and a side chain represented by the letter "R". The side chain can vary among different amino acids, giving them distinct chemical properties. The central carbon atom (alpha carbon) connects the amino group, carboxyl group, and the side chain, forming the backbone of the amino acid.
The isoelectric point of an amino acid is?
An amino acid is considered to be at its isoelectric point when the positive charges on the molecule exactly balance its negative charges. At this point, the amino acid carries no net charge and is therefore immobile in an electric field. Isoelectric points of amino acids widely vary accoriding to their side chains and polarity characteristics.
Which three components are common to all amino acids?
The 20 amino acids vary in structure by the R-group, otherwise all amino acids are the same in structure. All amino acids have a carboxyl group, an amino group, an R-group, and a hydrogen which are all bonded to a central carbon. It is the R-groups that make the amino acids react in different ways and alter the structure of the protein.
Can proteins form polymers?
Yes, proteins are formed from amino acid monomers. The OH group on one end of the amino acid bonds with the hydrogen group on the other end to form a water molecule. Then the peptide bond forms (carbon-nitrogen-carbon)
At Ph 10 what charge would Zwitterion ion have?
it would depend on amino acid in question. pH above amino acid pI, zwitterion will carry net negative (-) charge. at pH below pI, zwitterion will carry net positive (+) charge. depending on the amino acid, some have more than one acidic or basic functional group. such functional groups can make the amino acid vary in net charge from 2- to 2+ if not more.
How can there be so many different types of proteins when there are only 23 different amino acids?
Proteins are really very diverse in terms of their amino acid composition. Proteins are coded in the DNA, the sequence of DNA (A, T, G, C) determines the fate of amino acids that join together to form a protein. so the bases of the DNA can make a diverse group of proteins. normally proteins from a same family (for example antibodies or kinases) share a conserved domains or amino acids although they differ in their specificity and function.
What determines the identity of an amino acid in a proteins?
Amino acids play central roles both as building blocks of proteins and as intermediates in metabolism. The 20 amino acids that are found within proteins convey a vast array of chemical versatility. The precise amino acid content, and the sequence of those amino acids, of a specific protein, is determined by the sequence of the bases in the gene that encodes that protein. The chemical properties of the amino acids of proteins determine the biological activity of the protein. Proteins not only catalyze all (or most) of the reactions in living cells, they control virtually all cellular process. In addition, proteins contain within their amino acid sequences the necessary information to determine how that protein will fold into a three dimensional structure, and the stability of the resulting structure. The field of protein folding and stability has been a critically important area of research for years, and remains today one of the great unsolved mysteries. It is, however, being actively investigated, and progress is being made every day.As we learn about amino acids, it is important to keep in mind that one of the more important reasons to understand amino acid structure and properties is to be able to understand protein structure and properties. We will see that the vastly complex characteristics of even a small, relatively simple, protein are a composite of the properties of the amino acids which comprise the protein.Essential amino acidsHumans can produce 10 of the 20 amino acids. The others must be supplied in the food. Failure to obtain enough of even 1 of the 10 essential amino acids, those that we cannot make, results in degradation of the body's proteins-muscle and so forth-to obtain the one amino acid that is needed. Unlike fat and starch, the human body does not store excess amino acids for later use-the amino acids must be in the food every day.The 10 amino acids that we can produce are alanine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine and tyrosine. Tyrosine is produced from phenylalanine, so if the diet is deficient in phenylalanine, tyrosine will be required as well. The essential amino acids are arginine (required for the young, but not for adults), histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. These amino acids are required in the diet. Plants, of course, must be able to make all the amino acids. Humans, on the other hand, do not have all the the enzymes required for the biosynthesis of all of the amino acids.Why learn these structures and properties?It is critical that all students of the life sciences know well the structure and chemistry of the amino acids and other building blocks of biological molecules. Otherwise, it is impossible to think or talk sensibly about proteins and enzymes, or the nucleic acids.
How does protein structure affect protein function?
The primary structure is simply a long chain of peptides (polypeptide chain). The peptide monomers are like letters in a long, long word (the polypeptide). The word, a product of the primary structure and the peptide bonding sequence means something - whether it be, "I'm a transport protein." or "I'm an enzyme!". So, the primary structure definitely dictates the function of a protein by the sequence of amino acids it has. The primary structure's sequence of amino acids also dictates how the polypeptide will form (its structure). The R-group on the amino acids, which varies, will cause an amino acid to be positive, negative, polar, or nonpolar. This will cause the peptide chain, after these amino acids have been put together through dehydration reactions, to attract/form bonds with each other differently, leading to specific structures based off of the primary structure of a protein. These bonds vary between hydrophobic interactions, van der Waals attractions, hydrogen bonds, disulfide bridges, and a couple of other bonds. These new bonds and formations result in the secondary and tertiary levels of structure
The 20 amino acids vary only in their?
lipid groups
What is the R-group of Alanine?
An R group is the chemical group attached to the alpha carbon in an amino acid. In proteins all amino acids have the same basic structure and vary only in their R group. There are 20 standard amino acids found in proteins, which all have different R groups. For example an amino acids with Hydrogen from its R group is glycine, and one carbon with 3 hydrogens (a methyl group) is the R group for alanine.
What do the 20 amino acids vary in?
The amino acids vary in the side groups, usually designated by "R" on the chemical structures for amino acids. The invariant parts are the amino group (NH2-), central (-CH-) group, and the carboxyl (-COOH) group. Connected to the central carbon on the (-CH-) group is a side group which is part that varies.
