Sequence Information of Proteins
Just as members in the same family often resemble each other, similarly structured molecules are often grouped in the same category. There are several methods of comparing amino acid sequencing and determining how closely they are related. A simple example is the sequence-comparison method. Sequence databases are searched for a specific amino acid sequence of unknown characteristics. A set of molecules that are similar in structure can give insight into the properties of the unknown sequence of amino acids.
To determine the similarity between 2 amino acid sequences, one can apply sequence alignment. This method aligns the 2 sequences and slides them past each other one amino acid at a time and calculates what position has the greatest amount of matched residues. However, there is a drawback to this method in that it does not show all of the possible alignments. To counteract this, one can induce a gap in one of the sequences to increase the total possibilities of matches. The gap will compensate for the insertions of deletions of sequences in a gene that is absent in the second sequence.
However, simply comparing the identities of amino acids cannot account for everything. To increase the accuracy in the comparing two sequences there are 2 kinds of substitutions that can be made to further progress the determination of amino acids. The first is a conservative substitution which substitutes one amino acid with another amino acid that is
There are six variant forms of an enzyme; one is normal and five are mutant. The normal enzyme has glutamine at amino acid position 150, which is on the protein surface. Each mutant form has an amino acid substitution at position 150 as indicated. Which mutant form is most likely to have an increase
The genetic code has 64 codons, which codes for 20 amino acids. Redundancies of the genetic code allow different variation of codons to code for the same amino acids. The benefit of this is that even if there is a mistake in the base pairing, the amino acid might be unaffected. This allows amino acids to be represented in more than one combination.
b. Explain the most likely genetic change that produced the polypeptide in Species III. The most likely genetic change to have occurred would have been a point mutation that coded a STOP codon which would have halted the production of the polypeptide prematurely, thus leaving the blank spaces where no amino acid is present. c. Compare the peptides from Species I and IV. Discuss the nature of the amino acid changes.
These procedures can solve many mysteries and questions. The DNA sequencing of different species can identify where it falls on the phylogenetic tree and where the population separated to produce a new species. These procedures help us understand the evolution of ancestors to the present and the connection between each species. Two separate species with multiple similarities can be observed, and bioinformatics can help answer that question.
In terms of comparing protein sequences, “homologous” means similarity between protein sequences. The proteins may be even more homologous because of similar – but not identical – residues. Often, homology is
As well as this, certain blood proteins are found in a number of species. When genetic code (DNA and RNA) is used by a cell, it builds amino acids in a sequence, which forms protein. Chemical tests can determine whether one species has the similar blood proteins to another, thus showing evidence of evolutionary relationships. Organisms with a common ancestor have a close number of amino acid sequences in common. For example, chimpanzees and humans have no difference in their amino acid protein count in their haemoglobin – evidence for a common ancestor.
Sometimes, this can be a difference of just one base pair. These differences are called polymorphisms and are the key to DNA typing.(3)
The percentage pairwise identity indicates the percentage of base pair matching between the unknown specimen and the search results. Because the gene is highly conserved it is unlikely to differ largely between different species so the percentage difference is likely to be high. Therefore a percentage greater than 95% is indicative of the same species whereas closely related species have a percentage result of 85-95%. The E-value is a measure of significance and is the number of results expected if the chance was acting alone. When the E-value is higher than 0.01 then it is likely chance is acting alone and if the E-value is low then it is likely chance is not acting alone and the hit result is a genuine hit. The results have been accumulated for each of the three unknown species and the results from the first ten hits have been recorded in each of the tables.
Proteins are primarily considered to have one primary function to serve its role in an organism, however studies have observed to have multiple functioning proteins known as moonlighting proteins (Khan et al. 2014). Moonlighting proteins along with primary functions, have secondary functions that are not related to the primary function and does not correlate to the primary or other functions (Khan et al. 2014). The multifunctional proteins play essential roles in carrying out biochemical functions which aids in the cell growth but are not caused by gene fusion and multiple RNA splice variants (Amblee et al. 2015). The discovery of moonlighting proteins was first discovered by Piatigorsky and Wistow while observing crystallins (Khan et al. 2014). Crystallins, are structural proteins that are found in the eye lens that exhibit enzymatic activity to make the lens itself (Khan et al. 2014). Crystallin has a primary function to help form the lens of the eye by acting as a structural protein (Amblee et al. 2015). Besides enzymatic activity, crystallin was observed in other mammals to have secondary functions such as metabolic functions which are helpful in prokaryotic (Khan et al 2014). Most moonlighting proteins are characterized as cytosolic enzymes and chaperons, or in other words helping proteins (Amblee et al 2015). The multifunctional proteins or moonlighting proteins can also be identified as receptors, channel proteins and ribosomal proteins (Khan et al. 2014). Due to the
Proteins are polymeric chains that are built from monomers called amino acids. All structural and functional properties of proteins derive from the chemical properties of the polypeptide chain. There are four levels of protein structural organization: primary, secondary, tertiary, and quaternary. Primary structure is defined as the linear sequence of amino acids in a polypeptide chain. The secondary structure refers to certain regular geometric figures of the chain. Tertiary structure results from long-range contacts within the chain. The quaternary structure is the organization of protein subunits, or two or more independent polypeptide chains.
DNA barcoding uses standard genetic markers to compare DNA sequences among existing species by scanning for polymorphisms in standard sequences to differentiate between species (Hartvig, 2015). It is effective in differentiating between phenotypically similar species and is applicable to all organisms of life (Dudu, 2016). For DNA barcoding, the DNA is isolated from a sample and standard genetic markers are amplified by Polymerase Chain Reaction (PCR). A polymorphism is differences in DNA sequence that accumulate over time (Albert, 2011). The main source of mutations occurs during DNA replication and, thus mutations can be inherited. When the frequency of the mutation increases, it can become fixed in a lineage (Albert, 2011). Polymorphisms can indicate common ancestry among individuals by comparing standardized sequences across a species (Stoneking, 2001). Specifically, one region in the
The first organism the Xenopus had a 90% alignment match, and had a 5% gap. The second organism the Danio rerio had an 89% match and a 5% gap. On the Mus musculus the amount that was a perfect match with the Homo sapiens was 91%, and the amount that was gaped was 7%.
The Functions of Proteins Introduction Protein accounts for about three-fourths of the dry matter in human tissues other than fat and bone. It is a major structural component of hair, skin, nails, connective tissues, and body organs. It is required for practically every essential function in the body. Proteins are made from the following elements; carbon, hydrogen, oxygen, nitrogen and often sulphur and phosphorus.
In choosing branched chain amino acids for my ergogenic aid project, I took a few different things into account. When looking at the list provided to our class for this project, I told myself that I wanted a challenge. I wanted to work on a topic that I knew very little about to begin with. Some of the choices off of the ergogenic aid list seemed to easy and broad. Options such as protein and alcohol would seem to be rather easy and bland. To begin with, I had heard of amino acids and branched chain amino acids. However, I knew next to nothing about them. Instead of covering the broad topic of all the amino acids, this topic allowed myself to go deeper