Ví dụ về việc sử dụng Tertiary structure trong Tiếng anh và bản dịch của chúng sang Tiếng việt
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Protein tertiary structure is the three dimensional shape of a protein.
The Quaternary Structure is formed by several tertiary structures together.
Tertiary structure comprises a three dimensional folding of the polypeptide chains resembling a tangled ball of yarn.
These coordinates may refer either to a protein domain orto the entire tertiary structure.
The science of the tertiary structure of proteins has progressed from one of hypothesis to one of detailed definition.
Lanthionine, similar with mono-sulfide link Protein tertiary structure Sullivan reaction Cystinosis.
The interactions andbonds of side chains within a particular protein determine its tertiary structure.
There is a commonality of stable tertiary structures seen in proteins of diverse function and diverse evolution.
The functional form of single stranded RNA molecules(like proteins)frequently requires a specific tertiary structure.
The tertiary structure will have a single polypeptide chain"backbone" with one or more protein secondary structures, the protein domains.
They have the ability to lead to coagulation and denaturation of whites,changing their spatial tertiary structure.
When pH drops below pH 5, micelles of caseins, a hydrophobic protein,loses its tertiary structure due to the protonation of its amino acid residues.
For example, in secreted proteins, which are not bathed in cytoplasm,disulfide bonds between cysteine residues help to maintain the tertiary structure.
Geometric models are used to examine tertiary structure of the nanostructures and to ensure that the complexes are not overly strained.[66][68].
If lysozyme is heated slowly, the heat energy will disrupt only the weak interactions andcause only the tertiary structure to break down.
This architecture, the"tertiary structure" of molecules, depends in a complicated way on each molecule's basic composition, or"primary structure.".
Rosetta@home consistently ranks among the foremost docking predictors,and is one of the best tertiary structure predictors available.[6].
The first tertiary structures to be determined took years to figure out, but today, dozens of new structures are published every week.
When such binding occurs the electrical charges on the protein chain change,causing the protein's tertiary structure(i.e. 3-dimensional form) to change.
This binding ability is mediated by the tertiary structure of the protein, which defines the binding site pocket, and by the chemical properties of the surrounding amino acids' side chains.
As mentioned earlier, many functional proteins contain two or more polypeptide chains, called subunits,each of them folded into its own unique tertiary structure.
A protein domain is aconserved part of a given protein sequence and tertiary structure that can evolve, function, and exist independently of the rest of the protein chain.
While hydrogen bonding between the N- H and C= O groups within and between chains is responsible for secondary structure, the interactions between R groups- the amino acid side chains-determine tertiary structure.
But the protein will return to its normal tertiary structure when it cools, demonstrating that all the information needed to specify the unique shape of a protein is contained in its primary structure. .
Membrane protein structures can be determined by X-ray crystallography, electron microscopy or NMR spectroscopy.[10]The most common tertiary structures of these proteins are transmembrane helix bundle and beta barrel.
Although the a helices and P pleated sheets contribute to the tertiary structure, only parts of the macromolecule usually have these secondary structures, and large regions consist of structures unique to a particular protein.
Phosphogluconolactonase(6PGL, PGLS) is a cytosolic enzyme found in all organisms that catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconic acid in theoxidative phase of the pentose phosphate pathway.[2] The tertiary structure of 6PGL employs an α/β hydrolase fold, with active site residues clustered on the loops of the α-helices.
Each contains twenty-one aminoacid residues that spontaneously fold into a defined tertiary structure with two interchain-cysteine linkages(disulfide bonds) and a long hydrophobic tail.[2] There are also other compounds, however, they are mostly derivations of previously mentioned ones.
The protein can be tested for enzymatic activity under a variety of situations,the protein may be crystallized so its tertiary structure can be studied, or, in the pharmaceutical industry, the activity of new drugs against the protein can be studied.