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TOK: This is an example of a paradigm shift, where existing ideas about the tolerance of bacteria to stomach acid were incorrect but persisted for a time despite the evidence.
Aim 7: Data logging with pH sensors and lipase, and data logging with colorimeters and amylase can be used. Check out our new site currently under development, combining the Biotechnology and Science Learning Hubs with a new look and new functionality.
Sucrose binds to the active site on sucrase, and this puts stress on the bond between the 2 sugars that make up sucrose. Ribonucleic acid (RNA) also consists of nucleotides, but these nucleotides contain the sugar ribose.
Protein synthesis is the process in which the correct amino acids are connected together in the order that is written on the gene. Messenger RNA carries genetic information from DNA to the cytoplasm where the amino acids will be connected together. Transfer RNA (tRNA) is a carrier molecule for amino acids, delivering them to the site of protein synthesis.
The two ribosomal RNA (rRNA) subunits join with proteins in the cytoplasm to form the subunits of ribosomes. Step 2- During translation, the correct amino acids are dropped off by tRNA's according to the instructions written on the mRNA. Within a gene, information for the amino acid sequence of a protein is encoded in a triplet code. Imagine if you had a recipe that used 3 letter abbreviations for the ingredients water, sugar and flour. The tRNA is a single-stranded RNA molecule with an amino acid bound to one end and an anticodon on the other end. The anticodon is complementary to the corresponding mRNA codon and can temporarily match up to it. As a mature mRNA moves to a ribosome, the sequence of codons in the mRNA determines the sequence of anticodons that can match up. The story of how the Australians Robin Warren and Barry Marshall made the discovery and struggled to convince the scientific and medical community is well worth telling. Proteins are one of the three most important classes of large biological molecules – nucleic acids, proteins and carbohydrates. The triplet code means that three bases are read at a time and each three bases stand for one of the twenty amino acids.
Bile molecules have a hydrophilic end and a hydrophobic end, and thus prevent lipid droplets coalescing.


To understand what is protein, one must know what is their structure, how they are synthesized, which are their primarily functions and particularly how they participate in the metabolism processes. The protein structure defines the protein primary function and determines the uniqueness of each protein. The need for lipase to be water-soluble and to have an active site to which a hydrophobic substrate binds should be mentioned. The specificity of the protein structure is dictated by the nucleotide sequence of corresponding genes which defines the actual amino acid sequence and composition. The order of amino acids and their interaction  results in specific folding of the protein and determines a particular three-dimensional structure that defines its activity.
All amino acids which build proteins have the three common structural features:  an ?-carbon to which an amino group a carboxyl group, a variable side chain are bondedThe first two determine the building of a repeatable and identical bonds between the amino acids, called peptide bond. When it becomes part of a protein chain, a single amino acid is called an amino acid residue or just residue. The single residues are linked to each other with series of carbon, nitrogen, and oxygen atoms known as protein backbone. While the side chains of the standard amino acids are quite variable in chemical structures and properties, which determines the specifics of the physico-chemical properties of the amino acids residues.
As proteins are linear biopolymers, their two ends could be easily distinguished – the protein end with a free carboxyl group is denoted as the carboxy- or C-terminus, while the other end with a free amino group is known as the amino- or N-terminus. The interaction of the amino acid side chains determines protein 3D-structure and its overall biochemical function.
The understand what is protein, polypeptide, or peptide one should capture the specifics of the term meaning and also to put in the particular context. The term protein is preferred in the cases when the complete biological molecule is in a stable conformation, while peptide is generally used when the molecule is a short amino acid oligomers (up to 20–30 residues) often without stable 3D-structure.
The term polypeptide stays in between – a variable in length sequence of amino acids, which does not have a defined conformation. The actual composition and order of the amino acids in the polypeptide chain is encoded in genes. The genetic code is based on nucleotide triple sets called codons as each codon codes for a specific an amino acid. For each amino acid, there is more than one codon, because nucleic acids have four different nucleotides, which make 64 possible codons. The information encoded in genes as part of the DNA are first transcribed by RNA polymerase and other enzymes into pre-messenger RNA (mRNA).
Using various types of post-transcriptional modification, most of the organisms process the pre-mRNA to form the mature mRNA, which can then be used as a pattern for protein synthesis by the ribosomes.


The process of protein synthesis from an mRNA is also known as translation.What Is Protein Function Proteins are among the main functional units within the cell, as they perform the functions encoded in genes. The complete set of proteins expressed in a particular cell or cell type is forms its proteome. The overall protein function has 3 main components: molecular function participation in biological process cellular localization Speaking simple, the function of a protein is defined when it is known what is its molecular function, in which biological processes the protein applies this molecular function and in which particular cellular localization they perform this function. Some of the main protein functions are dependent of the their ability to bind with other molecules specifically.
Proteins have one or more regions responsible for binding another molecule, called binding site or "pocket". In case when proteins bind specifically to other molecules of the same type, they oligomerize and form fibrils, which is quite common for the structural proteins.
Based on the protein main functional characteristics and their participation in major biological processes, we can distinguish the following main protein types:Enzymes are the most abundant and best-known type of proteins in the cell. They catalyze different biochemical reactions in the cell which are part of major biological processes. The enzyme molecules usually bind highly specific to their substrates and catalyze only one or, rarely, a few biochemical reactions.Cell signaling and ligand binding - Many proteins participate in the process of cell signaling and signal transduction. Some proteins called as hormones, such as insulin, transmit signals from the cell in which they were synthesized to other distant cells, tissues and organs. There are some membrane proteins receptors which primary function is to bind an external to the cell signaling molecule and induce a response in the cell.Antibodies are proteins, which in the adaptive immune response have the main function to bind foreign substances, called antigens, and initiate their destruction.
Antibodies are secreted into the extracellular matrix or anchored in the B-cells cellular membranes (plasma cells).Transport proteins bind specific small molecules and transfer them to other locations in the body. A classical example of a transport protein is haemoglobin, which transports oxygen from the lungs to other organs and tissues in all vertebrates. Transport proteins are required to have a high binding affinity when their ligand is abundant and to release the ligand when it is in low concentrations in the target location.Trans-membrane proteins can also serve as ligand transport proteins that alter the permeability of the cell membrane to small molecules and ions. The membrane alone has a hydrophobic core through which polar or charged molecules cannot diffuse.



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