What type of molecular chaperone, sometimes called a chaperonin, forms a large, barrel-shaped 'isolation chamber' for the protein folding process?
Explanation
Cells have different classes of molecular chaperones. The hsp60 family, or chaperonins, are distinctive in that they provide a sequestered environment, an 'isolation chamber,' where a single polypeptide chain can fold without the risk of aggregating with other proteins.
Other questions
What is the name of the principle that describes the flow of genetic information from DNA to RNA (transcription) and from RNA to protein (translation) in all living cells?
What are the two principal chemical differences between RNA and DNA molecules?
According to the text, what is the approximate error rate for RNA polymerase during transcription?
In bacterial transcription, what is the primary function of the sigma (σ) factor?
Which eukaryotic RNA polymerase is responsible for transcribing the genes for transfer RNA (tRNA), 5S rRNA, and some small RNAs?
What is the first modification that occurs on a eukaryotic pre-mRNA molecule as it is being synthesized by RNA polymerase II?
During the process of pre-mRNA splicing, what is the name of the looped structure formed by the excised intron?
What is the primary catalytic component of the spliceosome, responsible for carrying out the chemical reactions of splicing?
The process by which a single gene can produce a set of different but related proteins by splicing the RNA transcript in multiple ways is known as what?
Approximately how many adenine (A) nucleotides are added to the 3' end of a eukaryotic mRNA by poly-A polymerase to form the poly-A tail?
What is the primary site of ribosome synthesis and assembly in a eukaryotic cell?
What is the term for a group of three consecutive nucleotides in an mRNA molecule that specifies either an amino acid or a stop to translation?
What is the function of transfer RNA (tRNA) molecules in protein synthesis?
The phenomenon where a tRNA molecule can base-pair with more than one codon, typically due to a mismatch being tolerated at the third position of the codon, is known as what?
What is the function of aminoacyl-tRNA synthetase enzymes?
The ribosome is a large complex primarily composed of what two types of macromolecules?
What are the names of the three binding sites for tRNA molecules within a ribosome?
The central reaction of protein synthesis, the formation of a peptide bond, is catalyzed by what component of the ribosome?
In eukaryotic translation initiation, what molecule is always carried by the special initiator tRNA?
What signals the termination of translation when it appears in the A site of the ribosome?
What is the name for the large cytoplasmic assemblies made up of several ribosomes that simultaneously translate a single mRNA molecule?
The quality-control mechanism that detects and degrades mRNAs containing a premature stop codon, often as a result of a splicing error, is called what?
What is the primary signal that molecular chaperones, such as hsp70, recognize on a misfolded or incompletely folded protein?
What small protein is attached in a chain to aberrant proteins to mark them for destruction by the proteasome?
What is the name of the central, hollow cylinder of the proteasome that contains the active sites for proteolysis?
According to the RNA world hypothesis, what dual role did RNA molecules play in primitive cells?
What is the key structural feature of eukaryotic RNA polymerase II that is absent in RNA polymerases I and III, and which is crucial for coordinating capping, splicing, and 3' end processing?
How many total possible combinations of three nucleotides (codons) are there in the genetic code, and how many different amino acids are commonly found in proteins?
During the elongation cycle of translation, how many high-energy phosphate bonds are consumed for each amino acid added to a polypeptide chain?
What is the role of guide RNAs, such as snoRNAs, in the processing of precursor ribosomal RNA (rRNA)?
How does the ribosome-associated quality control (RQC) system typically handle a ribosome that has stalled at the end of a broken mRNA molecule?
In bacteria, what is the role of the Shine-Dalgarno sequence?
How many tandem repeats of a seven-amino-acid sequence does the C-terminal domain (CTD) of human RNA polymerase II consist of?
In the process of regulated destruction, what is the role of the 19S cap of the proteasome?
What is the approximate rate of translation in a eukaryotic ribosome versus a bacterial ribosome?
When a human cell is not actively dividing, what percentage of its RNA is ribosomal RNA (rRNA)?
Which type of noncoding RNA directs the splicing of pre-mRNA to form mRNA?
What does the TATA-binding protein (TBP), a subunit of the general transcription factor TFIID, do upon binding to the TATA box sequence in DNA?
Why is the genetic code described as being redundant?
What is the typical length of a tRNA molecule?
Which process is NOT a recognized quality-control mechanism used by cells to prevent the translation of damaged or aberrant mRNAs?
What is the primary energy source that drives the conformational changes in elongation factors like EF-Tu and EF-G, and also powers the threading of proteins into the proteasome by AAA proteins?
What is a 'ribozyme'?
What are the key consensus sequences that signal the beginning and end of most introns in human pre-mRNAs?
In the four-step elongation cycle of translation, what immediately follows the formation of a new peptide bond in step 2?
How do many antibiotics, such as tetracycline and chloramphenicol, function to combat bacterial infections?
Why did the existence of introns in eukaryotic genes come as a surprise to scientists in 1977?
What is the primary reason that DNA is a more stable molecule for storing genetic information than RNA?
Approximately what percentage of the total proteins in a cell do proteasomes constitute?