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Page "Protein" ¶ 2
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polypeptide and is
A polypeptide is an unbranched chain of amino acids.
In Mycobacterium tuberculosis, the AC-III polypeptide is only half as long, comprising one 6-transmembrane domain followed by a cytoplasmic domain, but two of these form a functional homodimer that resembles the mammalian architecture.
The convention for a polypeptide is to list its constituent amino acid residues as they occur from the amino terminus to the carboxylic acid terminus.
A beta strand ( also β strand ) is a stretch of polypeptide chain typically 3 to 10 amino acids long with backbone in an almost fully extended conformation.
The pyrrolidine rings keep out of each other ’ s way when the polypeptide chain assumes this extended helical form, which is much more open than the tightly coiled form of the alpha helix.
They signal release of the nascent polypeptide from the ribosome because there is no cognate tRNA that has anticodons complementary to these stop signals, and so a release factor binds to the ribosome instead.
The amino acid sequence of any polypeptide created by a cell, is in turn determined by the stretches of DNA called genes.
An mRNA molecule is said to be monocistronic when it contains the genetic information to translate only a single protein chain ( polypeptide ).
On the other hand, polycistronic mRNA carries several open reading frames ( ORFs ), each of which is translated into a polypeptide.
The growing polypeptide is often termed the nascent chain.
A polypeptide is a long, continuous, and unbranched peptide.
* A polypeptide is a single linear chain of amino acids.
* An oligopeptide ( or simply a peptide ) is a polypeptide less than 30-50 amino acids long.
It is attached to the polypeptide C-terminus through an amide linkage that then connects to ethanolamine, thence to sundry sugars and finally to the phosphatidylinositol lipid moiety.
* Intermolecular transesterification can transfer a whole segment from one polypeptide to another, as is seen in the Hedgehog protein autoprocessing.
The last version is used as a template in synthesis of a polypeptide chain.
In translation, messenger RNA ( mRNA ) is decoded to produce a specific polypeptide according to the rules specified by the trinucleotide genetic code.
Translation proceeds in four phases: activation, initiation, elongation, and termination ( all describing the growth of the amino acid chain, or polypeptide that is the product of translation ).
This polypeptide is subsequently cleaved into individual polypeptide chains.
To form the mature insulin, the proinsulin is then cleaved at two positions to yield two polypeptide chains linked by 2 disulphide bonds.
Proinsulin is necessary for the folding of the polypeptide chain as the 2 polypeptide chains of insulin may not correctly assemble into the correct form while its precursor proinsulin do.
In secretory proteins and type I transmembrane proteins, the signal sequence is immediately cleaved from the nascent polypeptide once it has been translocated into the ER by signal peptidase.

polypeptide and single
Protein, though used colloquially to refer to any polypeptide, refers to larger or fully functional forms and can consist of several polypeptide chains as well as single chains.
Pre-pro-lactase, the primary translation product, has a single polypeptide primary structure consisting of 1927 amino acids.
Mature human lactase consists of a single 160 kDa polypeptide chain that localizes to the brush border membrane of intestinal epithelial cells.
* Quaternary structure: the structure formed by several protein molecules ( polypeptide chains ), usually called protein subunits in this context, which function as a single protein complex.
Many viruses also produce their proteins initially as a single polypeptide chain that were translated from a polycistronic mRNA.
Influenza hemagglutinin, for example, is synthesized as a single polypeptide chain that acts as a kinetic trap.
The viral proteins are transcribed as a single, long polypeptide, which is cleaved into the structural and nonstructural viral proteins.
The thaumatin protein I consists of a single polypeptide chain of 207 residues.
In prokaryotes and eukaryotes, it is an enzyme that consists of two polypeptide chains, a heavy and a light subunit, processed from a single chain precursor by an autocatalytic cleavage.
The TSST-1 is secreted as a single polypeptide chain.
This is distinct from a multienzyme polypeptide, in which multiple catalytic domains are found in a single polypeptide chain.
The protein is secreted as a single glycosylated polypeptide, and cleavage of a signal sequence is required for its activity.
A single point mutation in this polypeptide chain, which is 147 amino acids long, results in the disease known as Sickle Cell Anemia .< ref name =" nature1 "> Suzanne.
Lymphocyte T-Cell Immunomodulator is a single chain polypeptide.
Glycophorin C ( GPC ) is a single polypeptide chain of 128 amino acids and is encoded by a gene on the long arm of chromosome 2 ( 2q14-q21 ).
Voltage-gated sodium channels and calcium channels are made up of a single polypeptide with four homologous domains.
In the monomer form, the enzyme is a single polypeptide chain, folded into eight strands of parallel α / β barrels, which surround a central deep pocket that is the active site.
Although synthesized as a single polypeptide chain, FXI circulates as a homodimer.
Humans and most eukaryotes have evolved an ACC with CT and BC catalytic domains and biotin carboxyl carrier domains on a single polypeptide.
The large size of the exposed protein macromolecule makes it similar to Neisseria gonorrhoeae outer membrane protein macromolecular complex, which implies that UspA may be a single polypeptide chain.

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