Build a concept map for a mature protein. Think about the road taken from a gene to a mature and normal functioning protein. Think about how it is made, processed, and set up to do its function for the cell. Focus on key things you know about the cell for the protein to be made and work properly and show these connections in the cell.
Mature protein;
Role of mature protein sequence in maltose binding protein;
Secretion of amber fragments of an E. coli periplasmic protein, the maltose-binding protein, was studied to determine if the mature portion of the protein is required for its export across the cytoplasmic membrane. A fragment lacking 25–35 amino acid residues at the C terminus is secreted at normal levels, suggesting that this sequence is not required for secretion. This is in contrast to the results obtained with the periplasmic protein β-lactamase. In studying another fragment of one-third the molecular weight of the intact protein, we found that the majority of the fragment is not recovered from the periplasmic fraction. However, a small amount of secretion of this polypeptide was observed. This fragment is synthesized as a larger molecular weight form when cells are induced for the synthesis of a maltose-binding protein-β-galactosidase hybrid protein, which was previously shown to block the proper localization and processing of envelope proteins. This result is consistent with the idea that the larger form is a precursor with an unprocessed signal sequence, whereas in the absence of the hybrid protein the fragment is a processed mature form. Thus secretion of the smaller fragment may be occurring up to the point where the signal sequence is removed. That this fragment has passed through the cytoplasmic membrane is further supported by its accessibility to externally added trypsin. We suggest that the fragment may be secreted to the periplasm, but cannot assume a water-soluble conformation; the majority of the polypeptide may be associated with the external surface of the cytoplasmic membrane. Thus the mature sequence of maltose-binding protein, at least its C-terminal two thirds, may not be required for its export across the cytoplasmic membrane
? Road taken from gene to a mature and normal function protein;
A gene directs the synthesis of a protein by a two-step process. First, the instructions in the gene in the DNA are copied into a messenger RNA (mRNA) molecule. The sequence of nucleotides in the gene determines the sequence of nucleotides in the mRNA. This step is called transcription.
Most genes contain the information needed to make functional molecules called proteins. (A few genes produce other molecules that help the cell assemble proteins.) The journey from gene to protein is complex and tightly controlled within each cell. It consists of two major steps: transcription and translation. Together, transcription and translation are known as gene expression.
During the process of transcription, the information stored in a gene's DNA is transferred to a similar molecule called RNA (ribonucleic acid) in the cell nucleus. Both RNA and DNA are made up of a chain of nucleotide bases, but they have slightly different chemical properties. The type of RNA that contains the information for making a protein is called messenger RNA (mRNA) because it carries the information, or message, from the DNA out of the nucleus into the cytoplasm.
Translation, the second step in getting from a gene to a protein, takes place in the cytoplasm. The mRNA interacts with a specialized complex called a ribosome, which "reads" the sequence of mRNA bases. Each sequence of three bases, called a codon, usually codes for one particular amino acid. (Amino acids are the building blocks of proteins.) A type of RNA called transfer RNA (tRNA) assembles the protein, one amino acid at a time. Protein assembly continues until the ribosome encounters a “stop” codon (a sequence of three bases that does not code for an amino acid).
The flow of information from DNA to RNA to proteins is one of the fundamental principles of molecular biology. It is so important that it is sometimes called the “central dogma.”

Function of protein;
| Table 1. Protein Types and Functions | ||
|---|---|---|
| Type | Examples | Functions |
| Digestive Enzymes | Amylase, lipase, pepsin, trypsin | Help in digestion of food by catabolizing nutrients into monomeric units |
| Transport | Hemoglobin, albumin | Carry substances in the blood or lymph throughout the body |
| Structural | Actin, tubulin, keratin | Construct different structures, like the cytoskeleton |
| Hormones | Insulin, thyroxine | Coordinate the activity of different body systems |
| Defense | Immunoglobulins | Protect the body from foreign pathogens |
| Contractile | Actin, myosin | Effect muscle contraction |
| Storage | Legume storage proteins, egg white (albumin) | Provide nourishment in early development of the embryo and the seedling |
Two special and common types of proteins are enzymes and hormones. Enzymes, which are produced by living cells, are catalysts in biochemical reactions (like digestion) and are usually complex or conjugated proteins. Each enzyme is specific for the substrate (a reactant that binds to an enzyme) it acts on. The enzyme may help in breakdown, rearrangement, or synthesis reactions. Enzymes that break down their substrates are called catabolic enzymes, enzymes that build more complex molecules from their substrates are called anabolic enzymes, and enzymes that affect the rate of reaction are called catalytic enzymes. It should be noted that all enzymes increase the rate of reaction and, therefore, are considered to be organic catalysts. An example of an enzyme is salivary amylase, which hydrolyzes its substrate amylose, a component of starch.
Build a concept map for a mature protein. Think about the road taken from a gene...
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PLEASE COMPUTER TYPED* OR VERY CLEAR HANDWRITING with
details
1. Radioactive (14C) uridine (lots of it) is added to a growing culture of bacteria for 10 seconds and then the drug rifamycin is added (rifamycin blocks the initiation of transcription, but not continued elongation of RNA polymerases that have already begun transcribing). At two-minute intervals, 1 ml samples are removed and placed on ice. The bacteria are lysed (broken open) and an enzyme is added that will chew up all...