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ionized. This doubly ionized form is called the zwitterion and overall has a
zero charge.
The compound glyceraldehyde is used as a reference compound for
distinguishing stereoisomers. It is the L-amino acids that are biologically
important, with very few exceptions. Amino acids found in proteins are
normally L-isomers. There are 20 common or major amino acids that are
found in proteins. They are divided into groups based on the nature of the
R group.
1. Nonpolar aliphatic R groups: The R group of these amino acids is
hydrophobic, but not the entire amino acid. Ex: Alanine, Valine,
Leucine, Isoleucine, Methionine (the R group contains sulfur),
Proline.
2. Aromatic R groups: the R groups of these amino acids are aromatic
and will absorb UV light at 280 nm. Ex: Phenylalanine, Tyrosine,
Tryptophan.
3. Polar, uncharged R groups (at pH = 7.0): Glycine (This is the only
amino acid without D and L forms), Serine, Threonine, cysteine (the
R group is a thoil or sulfydryl group), Asparagine, Glutamine.
4. Negatively-charged R groups (at PH = 7.0): these amino acids are
acidic and contain an extra carboxyl group. Aspartate, glutamate,
5. Positively-charged R groups (at pH = 7.0): These amino acids are
basic and contain an extra basic group. Lysine, Arginine, Histidine.
Another 300 amino acids have been found in biological systems that have
functions other than as protein components. They are a variety of
functions as precursors in biosynthesis and intermediates in metabolic
pathways.
Both the carboxy group and the amino acid (and sometimes the R-group)
have acid-base properties, so amino acids have complicated acid-base
behavior. These properties are crucial in determining the behavior of both
individual amino acids and the proteins that contain them.
A weak acid can be titrated with a strong base, and the pH of the resulting
solution plotted as a function of the amount of base added. At very low
pH, the amino acid will be in the fully protonated form. As base is added,
the COOH group will be titrated to COO-. When the half-equivalence point
has been reached, half the COOH has been converted to COO-. As more
base is added, the NH3+ group is titrated to NH2.
When the amino acid has no net charge, so this is called the isoeletric
point or isoionic point (PI).
Amino acid can join together to form polymers. When a few amino acids
are joined together, the molecule is called a peptide. When more amino
acids are joined together, the molecule is called a protein. The covalente
linkage between amino acids is called a peptide bond, which is chemically
an amide bond. There is restricted rotation around the peptide bond. The
configuration around a peptide bond is normally trans.
Peptides are named according to the amino acids components, beginging
with the N-terminal and ending with the C-terminal.
Peptide bonds stable under biological conditions. Peptide bonds can be
hydrolyzed by heating in strong acid or strong base. Peptide bonds can be
broken by a group of enzymes known as proteases.
Peptides are composed of L-amino acids, so they will be optically active.
There will be some pH, however, where the negative charges balance the
positive charges, and the peptide has no net charge. This point will be the
peptide’s isoelectric point.
Some hormones are peptides, such as insulin and glucagon. Some toxins
and antibiotics are peptides.
Proteins are the same as peptides, only larger with more amino acids. The
amino acids are still joined in a long, linear chain by peptide bonds. Some
proteins consist of a single polypeptide chain, but many of the large
proteins consist of two or more polypeptide chains associated together.
Such proteins are called multimeric or multisubunit proteins, and the
individual polypeptide chains are called subunits. The subunits may be
identical or they may be of different types.
Many proteins consist only of amino acids, but some contain a non-amino-
acid component called a prosthetic group. Some prosthetic groups are
small organic molecules related to vitamins, some are lipids (lipoproteins),
some are carbohydrates (glycoproteins), and some are metal atoms or
ions (metalloproteins). The prosthetic group is usually important for the
protein to function properly.
Enzimas
Função básica: catalisar as reações bioquímicas, diminuindo as energias de
ativação das reações.
A esmagadora maioria das reações bioquímicas dá-se em vias metabólicas,
que são sequências de reações em que o produto de uma reação é
utilizado em seguida como reagente na reação seguinte.
Um pequeno grupo de enzimas, as riboenzimas, têm uma natureza não-
proteica. As riboenzimas são moléculas de RNA que possuem capacidade
catalítica.
À parte dos sítios ativos das enzimas, onde os substratos se ligam para
sofrerem os efeitos catalíticas das enzimas, há também os centros
alostéricos aos quais determinadas espécies químicas se ligam,
modulando a atividade da enzima.
Algumas enzimas necessitam da presença de outras espécies químicas,
genericamente denominadas de cofatores, para efetuar a catálise. A
natureza química desses cofatores é diversa, podendo ser íons metálicos
(como Mg++, Zn+ ou ainda o Fe++), moléculas orgânicas ou também
vitaminas (como a vitamina B12). Em casos onde o grupo prostético é uma
molécula orgânica complexa demais, ela é chamada de coenzima.
O que define o sítio ativo da enzima onde o substrato vai se ligar é a
composição de aminoácidos do sítio, carga elétrica total, hidrofobicidade,
etc. São esses fatores que condicionam o tipo de substrato que pode ligar-
se ao centro ativo.
As enzimas são específicas para o seu substrato, catalisando uma só
reação. Existem algumas enzimas que catalisam substratos similares, mas
são mais específicas para um deles.
Classes de Enzimas:
1. Oxidorredutases: catalisam reações de oxirredução, transferindo
elétrons.
2. Transferases: transferem grupos químicos entre moléculas.
3. Hidrolases: Utilizam a água na reação catalítica.
4. Liases: formam ou destroem ligações duplas, respectivamente
retirando ou adicionando grupos funcionais.
5. Isomerases: Transformar uma molécula no seu isômero.
6. Ligases: formam ligações químicas por reações de condensação,
consumindo energia sob a forma de ATP.