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Page "Protein tertiary structure" ¶ 3
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Proteins and due
Proteins due to be translocated to the endoplasmic reticulum are recognized by the signal-recognition particle ( SRP ), which halts translation of the polypeptide by the ribosome while it attaches the ribosome to the SRP receptor on the endoplasmic reticulum.

Proteins and they
Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.
Proteins are also necessary in animals ' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food.
Proteins are classified by the folds they represent in databases like SCOP and CATH.
Proteins are vital parts of living organisms, as they are the main components of the physiological metabolic pathways of cells.
Proteins are separated according to isoelectric point ( pH at which they have neutral net charge ) in the first dimension, and according to their molecular weight in the second dimension.
Proteins are designated H ( hemagglutinin ) for morbilliviruses as they possess haemagglutination activity, observed as an ability to cause red blood cells to clump in laboratory tests.
Therefore, they have been assigned to the same superfamily in Structural Classification of Proteins ( SCOP ).
* Proteins are usually too big to pass through the kidneys, but they can pass through when the glomeruli are damaged.
Proteins homologous to σ < sup > 54 </ sup >/ RpoN are functional sigma factors, but they have significantly different primary amino acid sequences.
Proteins are placed in the same protein domain if they are isoforms of each other, or if they are essentially the same protein, but from different species.
Proteins constitute 90-95 % of venom's dry weight and they are responsible for almost all of its biological effects.
Proteins are classified as chemokines according to shared structural characteristics such as small size ( they are all approximately 8-10 kilodaltons in size ), and the presence of four cysteine residues in conserved locations that are key to forming their 3-dimensional shape.
Proteins are synthesized within the cell body, and hence they must travel along the axon to reach their final destination.

Proteins and fold
Proteins of very different amino acid sequences may fold into a structure that produces the same active site.
* Protein fold refers to the general protein architecture, like helix bundle, beta-barrel, Rossman fold or different " folds " provided in the Structural Classification of Proteins database .< ref name =" Govindarajan ">
Proteins ' need to fold correctly is a big restriction on the evolution of protein sequences.

Proteins and into
Proteins are ferried into the matrix via the translocase of the inner membrane ( TIM ) complex or via Oxa1.
Proteins ( or ) are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function.
Proteins can be informally divided into three main classes, which correlate with typical tertiary structures: globular proteins, fibrous proteins, and membrane proteins.
Proteins can also bind to, or even be integrated into, cell membranes.
Proteins do not have to unfold to be imported into the peroxisome.
Proteins in cells are also constantly being broken down into amino acids.
Proteins may be incorporated into the plasma membrane, or either trapped in the periplasm or secreted into the environment, according to whether or not there is an outer membrane.
Proteins that are formed from free ribosomes are released into the cytosol and used within the cell.
Proteins found in the tonoplast ( aquaporins ) control the flow of water into and out of the vacuole through active transport, pumping potassium ( K < sup >+</ sup >) ions into and out of the vacuolar interior.
Proteins are inserted into the membrane via the SRP-dependent pathway ( 1 ), the Tat-dependent pathway ( 2 ), or spontaneously via their transmembrane domains ( not shown in figure ).
Proteins are broken down into smaller components and these are excreted by the bacteria.
Proteins that contain zinc fingers ( zinc finger proteins ) are classified into several different structural families.
Proteins secreted through the type II system, or main terminal branch of the general secretory pathway, depend on the Sec or Tat system for initial transport into the periplasm.
Proteins which use this pathway have the capability to form a beta-barrel with their C-terminus which inserts into the outer membrane, allowing the rest of the peptide ( the passenger domain ) to reach the outside of the cell.
Proteins are introduced into a Immobilized pH gradient gel composed of polyacrylamide, starch, or agarose where a pH gradient has been established.
Proteins are classified into the chemokine family based on their structural characteristics, not just their ability to attract cells.
Proteins gain entry into the nucleus through the nuclear envelope.

Proteins and are
Proteins are very large molecules – macro-biopolymers – made from monomers called amino acids.
Proteins are condensation polymers made from amino acid monomers.
Proteins that function in the cytoplasm are often degraded by proteasomes.
Proteins are amino acid polymers.
Proteins provide amino acids, which are required for cell construction, especially for the construction of muscle cells.
Proteins are separated by charge in agarose because the pores of the gel are too large to sieve proteins.
IGF-1 and IGF-2 are regulated by a family of proteins known as the IGF-Binding Proteins.
Currently, there are six characterized IGF Binding Proteins ( IGFBP-1 to IGFBP-6 ).
Proteins that are needed in a particular region of the cell can also be translated there ; in such a case, the 3 ' UTR may contain sequences that allow the transcript to be localized to this region for translation.
Proteins are the basis of many animal body structures ( e. g. muscles, skin, and hair ).
Proteins that are sequestered in the nucleolus are unable to diffuse and to interact with their binding partners.
Proteins showing prion-type behavior are also found in some fungi, which has been useful in helping to understand mammalian prions.
Proteins are assembled from amino acids using information encoded in genes.
Proteins are always biosynthesized from N-terminus to C-terminus.
Proteins are not entirely rigid molecules.
Proteins are the chief actors within the cell, said to be carrying out the duties specified by the information encoded in genes.
Proteins consist of one or more polypeptides arranged in a biologically functional way and are often bound to cofactors, or other proteins.
Proteins are often synthesized in an inactive precursor form ; typically, an N-terminal or C-terminal segment blocks the active site of the protein, inhibiting its function.
Proteins that are to be targeted to a particular organelle or for secretion have an N-terminal signal peptide that directs the protein to its final destination.

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