Protein Synthesis
Protein synthesis is one of the most fundamental biological processes. To start off, a protein is made in a ribosome. There are many cellular mechanisms involved with protein synthesis. Before the process of protein synthesis can be described, a person must know what proteins are made out of. There are four basic levels of protein organization. The first is primary structure, followed by secondary structure, then tertiary structure, and the last level is quaternary structure. Once someone understands the makeup of a protein, they can then begin to learn how elements can combine and go from genes to protein. There are two main processes that occur during protein synthesis, or peptide formation. One is transcription and the other is translation. Although these biological processes slightly differ for eukaryotes and prokaryotes, they are the basic mechanisms for which proteins are formed in all living organisms.
There are four main levels of a protein, which make up its native conformation. The first level, primary structure, is just the basic order of all the amino acids. The amino acids are held together by strong peptide bonds. The next level of protein organization is the secondary structure. This is where the primary structure is repeated folded so that it takes up less space. There are two types of folding, the first of which is beta-pleated sheets, where the primary structure would resemble continuous spikes forming a horizontal strip. The seco...
Macromolecules are define as large molecules of structures found in living organisms. There are four types of macromolecules, which are proteins, carbohydrate, nucleic acid, and lipids also known as fats. Carbohydrates, proteins, and nucleic acids are made of monomers, which are structural units that eventually attached together to form polymers (Dooley 20). For instance, proteins are made of amino acids, which are monomers. In addition, it has a complex structure, which consist of four different levels, primary, secondary, tertiary, and quaternary. The first structure of protein is the primary structure, which is the sequence of amino acid, while in the secondary structure alpha and beta helices are formed. The structure, in which a protein becomes active, is in the tertiary structure, which is where polypeptide subunits fold. Meanwhile, only certain proteins have the quaternary structure, which is when, more than one polypeptide folds. Proteins are prominent macromolecules mainly because of their numerous functions. For instance, proteins are known for increasing the rate of reactions due to that enzymes are a type of protein. In addition, they are a form of defense mechanism such as they attack pathogens, which cause diseases. In other words, scientists study and gain more insight on certain illness and how to prevent them by using proteins. For example, in a recent study,
Sequence and structural proteomics involve the large scale analysis of protein structure. Comparison among the sequence and structure of the protein enable the identification on the function of newly discovered genes (Proteoconsult, n.d.). It consists of two parallel goals which one of the goals is to determine three-dimensional structures of proteins. Determine the structure of the protein help to modeled many other structures by using computational techniques (Christendat et al., 2000). This approach is useful in phylogenetic distribution of folds and structural features of proteins (Christendat et al., 2000). Nuclear magnetic resonance (NMR) spectroscopy is one of the techniques that provide experimental data for those initiatives. It is best applied to proteins which are smaller than 250 amino acids (Yee et al., 2001). Although it is limited by size constraints and also lengthy data collection and analysis time, it is still recommended as it can deliver strong results. There are two types of NMR which are one-dimensional NMR and two-dimensional NMR. One-dimensional NMR provides enough information for assessing the folding properties of proteins (Rehm, Huber & Holak, 2002). It also helps to identify a mixture of folded and unfolded protein by observing both signal dispersion and prominent peak. Observation in one-dimensional spectrum also obtains information on molecular weight and aggregation of molecule under investigation. In spite of this, two-dimensional NMR are used for screening that reveal structural include binding, properties of proteins. It also provides important information for optimizing conditions for protein constructs that are amenable to structural studies (Rehm et al., 2002). NMR is a powerful tool which it w...
Protein synthesis consists of two main steps: transcription and translation. The DNA is found inside of the nucleus and there in the nucleus a copy of one side of the DNA strand is made, this is the messenger RNA or mRNA. After this the mRNA travels through the cytoplasm with the DNA copy and arrives at the ribosomes. The mRNA then goes through the ribosome three bases at a time. A transfer RNA molecule or tRNA then bring the correct amino acid to match the codon. The amino acids then link together to form a long chain of proteins, making amino acids the building blocks of
“Proteins are large, complex molecules that play many critical roles in the body” (Genetics Home Reference, 2014, p. xx-xx). “They do most of the work in cells and are required for the structure, function, and regulation of the body’s tissues and organs” (Genetics Home Reference, 2014, p. xx-xx). “Proteins are made up of hundreds or thousands of smaller units called amino acids, which are attached to one another in long chains” (Genetics Home Reference , 2014, p. xx-xx). “There are 20 different types of amino acids that can be combined to make a protein” (Genetics Home Reference, 2014, p. xx-xx). “The sequence of amino acids determines each protein’s unique 3-dimensional structure and its specific function” (Genetics Home Reference, 2014, p. xx-xx).
Proteins are created from amino acids, and there are only to ways for our body to create them. They can be made from scratch or by modifying or altering other amino acids. A few essential amino acids can only be gotten from foods, there for high protein food choices certainly play a role in our health and wellbeing .
The process of translation is a major part of protein synthesis. There are many different components related the process of protein synthesis which include the large ribosomal unit, 60S and the small ribosomal unit,40S. As well as these are the messenger RNA, “mRNA coding”, transfer RNA , tRNA for amino acids and finally greater than 12 of the catalytic proteins which have be found to be eIFs (eukaryotic initiation factors). (Norton and Layman, 2006)These initiation factors are quite important in relation to Protein Synthesis and translation initiation. ...“These initiation factors guide the assembly of the ribosome on the mRNA and are responsive to short-term changes in the availability of energy, amino acids, and growth factors. Initiation factors provide the cell with sensitivity to environmental factors, including changes in diet, such as leucine availability, and physical activity.”... As well as this they also enable the cell to become sensitive to factors like the availability of
Proteins are one of the main building blocks of the body. They are required for the structure, function, and regulation of the body’s tissues and organs. Even smaller units create proteins; these are called amino acids. There are twenty different types of amino acids, and all twenty are configured in many different chains and sequences, producing differing protein structures and functions. An enzyme is a specialized protein that participates in chemical reactions where they serve as catalysts to speed up said reactions, or reduce the energy of activation, noted as Ea (Mader & Windelspecht).
Proteins are the building blocks of muscle. Protein synthesis is the process of building new proteins. This process happens at a cellular level.
In the hierarchial organisation of proteins, domains are found at the highest level of tertiary structure. Since the term was first used by Wetlaufer (1973) a number of definitions exist reflecting author bias, however all of the definitions agree that domains are independently folding compact units. Domains are frequently coded by exons and therefore have specific functionality. Among the many descriptions of protein domains the two most striking and simple are " Protein evolutionary units" and "Basic currency of Proteins".
What is protein and how is it made you ask. Well I will tell you first off i'm going to talk to you about DNA and life. Scientists thought that DNA was made up of four nucleotides, so the DNA was exactly the same(Nowicki, 2015). DNA contains the instructions on how to make all of our protein. Central dogma explains the patterns on how DNA goes to RNA to make protein. Central dogma goes from DNA to making new DNA. From DNA to make new RNA from RNA to make new proteins.
With the activation of a transcription factor, protein could be produced. With the production of protein, cellular respiration could then occur from the activation of the cell cycle.
Alu elements are the most abundant type of retrotransposable element, and are incorporated into the genetic sequence in a copy and paste manor. ~10.7% of the genome consists of Alu elements[1]. The large amount of Alu elements in the human genome results because of how they are replicated by LINE retrotransposons[2]. After replication they look similar to RNA Polymerase III replicated DNA, or mRNA, but they are reverse transcribed from the like-mRNA sequence into a newly created Alu element that can be transposed to a target sequence in the genome. Due to the vast amount of Alu elements, they contribute to genetic diversity and disease by inserting into sensitive portions of the genome that can result in mutagenesis. In my chosen case study,
Antimicrobial drugs that block protein synthesis react with ribosomal-mRNA complexes. These drugs are safe only because bacterial ribosomes are different in size and structure compared to human ribosomes, however, they can damage human mitochondria since they can contain ribosomes like bacterial ribosomes.
When eaten, protein is broken down into amino acids. Proteins and amino acids are used for almost every metabolic process in the body, and are the building blocks for every tissue in your body.
A polypeptide chain is a series of amino acids that are joined by the peptide bonds. Each amino acid in a polypeptide chain is called a residue. It also has polarity because its ends are different. The backbone or main chain is the part of the polypeptide chain that is made up of a regularly repeating part and is rich with the potential for hydrogen-bonding. There is also a variable part, which comprises the distinct side chain. Each residue of the chain has a carbonyl group, which is good hydrogen-bond acceptor, and an NH group, which is a good hydrogen-bond donor. The groups interact with the functional groups of the side chains and each other to stabilize structures. Proteins are polypeptide chains that have 500 to 2,000 amino acid residues. Oligopeptides, or peptides, are made up of small numbers of amino acids. Each protein has a precisely defined, unique amino acid sequence, referred to as its primary structure. The amino acid sequences of proteins are determined by the nucleotide sequences of genes because nucleotides in DNA specify a complimentary sequence in RNA, which specifies the amino acid sequence. Amino acid sequences determine the 3D structures of proteins. An alteration in the amino acid sequence can produce disease and abnormal function. All of the different ways