Background A tumor marker is a substance such as a protein, antigen or hormone in the body that may indicate the presence of cancer. Generally, these markers are specific to certain types of cancer and can be detected in blood, urine and tissue samples. The body may produce the marker in response to cancer or the tumor itself may produce the marker. The detection of tumor markers may be used to determine a diagnosis or as an indicator of disease cancer progression.
Primary, Secondary, Tertiary,… Proteins are the largest and most varied class of biological molecules, and they show the greatest variety of structures. The function of proteins depends on their structure, and defining the structure of individual proteins is a large part of modern Biochemistry and Molecular Biology.
To understand how proteins fold, we will start with the basics of structure, and progress through to structures of increasing complexity. This bond is formed between the alpha amino group of one amino acid and the carboxyl group of another in a condensation reaction.
When two amino acids join, the result is called a dipeptide, three gives a tripeptide, etc. Another property of peptides is polarity: In the natural course of making a protein, polypeptides are elongated by the addition of amino acids to the C-terminal end of the growing chain.
Conventionally, peptides are written N-terminal first; therefore gly-ser is not the same as ser-gly or GS is not the same as SG. If stretched out, the side chains of the individual residues project outwards from this backbone.
The peptide bond is written as a single bond, but it actually has some characteristics of a double bond because of the resonance between the C-O and C-N bonds: This means that the six atoms involved are coplanar, and that there is not free rotation around the C—N axis.
This constrains the flexibility of the chain and prevents some folding patterns. Primary Structure of Proteins It is convenient to discuss protein structure in terms of four levels primary to quaternary of increasing complexity. Primary structure is simply the sequence of residues making up the protein.
Thus primary structure involves only the covalent bonds linking residues together. The minimum size of a protein is defined as about 50 residues; smaller chains are referred to simply as peptides.
So the primary structure of a small protein would consist of a sequence of 50 or so residues. Even such small proteins contain hundreds of atoms and have molecular weights of over Daltons Da. There is no theoretical maximum size, but the largest protein so far discovered has about 30, residues.
Since the average molecular weight of a residue is about Da, that single chain has a molecular weight of over 3 million Daltons. Various types of secondary structure have been discovered, but by far the most common are the orderly repeating forms known as the a helix and the b sheet.
An a helix, as the name implies, is a helical arrangement of a single polypeptide chain, like a coiled spring. In this conformation, the carbonyl and N-H groups are oriented parallel to the axis. Each carbonyl is linked by a hydrogen bond to the N-H of a residue located 4 residues further on in the sequence within the same chain.
The alpha helix has precise dimensions: The side chains project outward and contact any solvent, producing a structure something like a bottle brush or a round hair brush. An example of a protein with many a helical structures is the keratin that makes up human hair. The structure of a b sheet is very different from the structure of an a helix.
In a b sheet, the polypeptide chain folds back on itself so that polypeptide strands like side by side, and are held together by hydrogen bonds, forming a very rigid structure.
Generally the primary structure folds back on itself in either a parallel or antiparallel arrangement, producing a parallel or antiparallel b sheet.
In this arrangement, side chains project alternately upward and downward from the sheet. The major constituent of silk silk fibroin consists mainly of layers of b sheet stacked on top of each another.
Other types of secondary structure. While the a helix and b sheet are by far the most common types of structure, many others are possible. These include various loops, helices and irregular conformations.
A single polypeptide chain may have different regions that take on different secondary structures. In fact, many proteins have a mixture of a helices, b sheets, and other types of folding patterns to form various overall shapes.
What determines whether a particular part of a sequence will fold into one or the other of these structures? A major determinant is the interactions between side chains of the residues in the polypeptide.
Several factors come into play:The DDBJ/ENA/GenBank Feature Table Definition Feature Table: Definition Version December DNA Data Bank of Japan, Mishima, Japan.
The ribosome (/ ˈ r aɪ b ə ˌ s oʊ m, -b oʊ-/) is a complex molecular machine, found within all living cells, that serves as the site of biological protein synthesis (translation). Ribosomes link amino acids together in the order specified by messenger RNA (mRNA) molecules. Ribosomes consist of two major components: the small ribosomal subunits, which read the RNA, and the large subunits.
Description and examples. Many proteins are actually assemblies of multiple polypeptide chains. The quaternary structure refers to the number and arrangement of the protein subunits with respect to one another. Examples of proteins with quaternary structure include hemoglobin, DNA polymerase, and ion channels..
Enzymes composed of subunits with diverse functions are sometimes called. Human Brain - Neuroscience - Cognitive Science The Human Brain is the most Complex Processer of Information on the torosgazete.com ability to Process Information and Store Information,, is what makes us torosgazete.comation Defines us, Information Controls us, Information Teaches us.
Know your Processor, understand the Software (), and understand the Hardware (). Shortly after or even during synthesis, the residues in a protein are often chemically modified by post-translational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins.
Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors.
What are proteins made up of? - Simple protein may just be on polypeptide chain - The combination of a number of different polypeptide chains and associated non-protein (prosthetic) groups into a large, complex protein molecule.
What do large protein often form?