| NOUN | a folded protein | folded proteins |
NOUN article.ind sg | pl
21 Übersetzungen
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- The shape of the folded protein can be used to understand its function and design drugs to influence the processes that it is involved in.
- Another co-chaperone, GrpE, comes in following the folding of this protein to cause a conformational change in DnaK that allows it to release the folded protein.
- The crowded environment of the cytosol can accelerate the folding process, since a compact folded protein will occupy less volume than an unfolded protein chain.
- Amino acids interact with each other to produce a well-defined three-dimensional structure, the folded protein (the right hand side of the figure), known as the native state.
- The first was that a change of the active site nucleophile of a glycosidase from a carboxylate to another amino acid resulted in a properly folded protein that had no hydrolase activity.
- It is made up of amino acid residues that are distant to one another in the primary sequence, but come close to each other in the tertiary structure of the folded protein (see red patch in the diagram).
- This irreversibility is typically a kinetic, not thermodynamic irreversibility, as a folded protein generally has lower free energy than when it is unfolded.
- The term "molten globule" may be used to describe various types of partially-folded protein states found in slightly denaturing conditions such as low pH (generally pH = 2), mild denaturant, or high temperature.
- A DNA-binding domain (DBD) is an independently folded protein domain that contains at least one structural motif that recognizes double- or single-stranded DNA.
- Most of the intrinsic fluorescence emissions of a folded protein are due to excitation of tryptophan residues.
- The folded protein complexes of interest separate cleanly and predictably due to the specific properties of the polyacrylamide gel.
- ... those below the length of 10 amino acids) may be intrinsically disordered, and not part of any folded protein domains.
- Post-translational modifications can incorporate more complex, large molecules into the folded protein structure.
- A chaperone protein (calnexin/calreticulin) binds to the unfolded or partially folded protein to assist protein folding.
- Amino acids widely separated in a protein's sequence may touch or lie very close to one another within a stably folded protein.
- Huntington's disease results from a mutation in either copy of the HTT gene, which results in an abnormally folded protein.
- These compounds are thought to act by binding to solvent-exposed hydrophobic segments of unfolded or improperly folded proteins, thereby “protecting” them from aggregation.
© dict.cc English-German dictionary 2024
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