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How do a polypeptide get into the ER for additional processing?
Polypeptides are directed to the endoplasmic reticulum (ER) during translation through a signal peptide that emerges from the ribosome. This signal peptide is recognized by the signal recognition particle (SRP), which halts translation and guides the ribosome to the ER membrane. Once there, the ribosome binds to the translocon, allowing the polypeptide to be threaded into the ER lumen for further processing, such as folding and post-translational modifications. After entry, the signal peptide is typically cleaved off, facilitating the maturation of the polypeptide.
What type of signal does a potentiometer produce?
A: Potentiometer does not produce any signal it is merely a variable resistor whereby any signal impressed on it can be variably taken out of the wiper as a linear function or logarithms function depending on the requirement of the design
What is a signaling function?
a signal source is a function it can be square , triangle sine and any combination of the three
What is definition of open loop transfer function?
According to 'Modern Control Engineering' written by Katsuhiko Ogata, the ratio fo the feedback signal, H(s)C(s)to the actuating error signal (R(s)-B(s)) is called the open-loop transfer function. Here, H(s) is the transfer function of the feedback signal detector, C(s) is the output signal and R(s) is the setpoint signal.
What is a non inverter?
It does what the name emply it changes the function or polarity OS a signal.
What are some identifiers for the c peptide?
The connecting peptide, or C-peptide, is a short 31-amino-acid protein that connects insulin's A-chain to its B-chain in the proinsulin molecule. In the insulin synthesis pathway, first preproinsulin is secreted from the beta cells of the pancreas with an A-chain, a C-peptide, a B-chain, and a signal sequence. The signal sequence is cleaved from the N-terminus of the peptide by a signal peptidase, leaving proinsulin. Then the C-peptide is removed, leaving the A-chain and B-chain that constitute the insulin molecule.
What is the difference between a cis and trans peptide bond?
A cis peptide bond occurs when the two amino acids in a peptide chain are on the same side of the peptide bond, while a trans peptide bond occurs when the two amino acids are on opposite sides of the peptide bond. This difference in orientation can affect the overall structure and function of the protein.
What is the function of the WR signal on the memory chip?
what is the function of the wr signal on memory chip
What is the difference between multichannel and multidimensional signals?
if a signal is a function of single independent variable,then signal is called multichannel signal. if a signal is function of multiple independent variable then signal is called multidimensional signal.
What are three hormones that can regulate kidney function?
ADH, Aldosterone and Atrial Natriuretic peptide(ANP)
What is the significance of a trans peptide bond in protein structure and function?
A trans peptide bond in protein structure is significant because it affects the protein's overall shape and stability. It can influence how the protein folds and interacts with other molecules, ultimately impacting its function in the body.
What is the first signal required for activation of a T cell?
The first signal required to activate a T cell is MHC(Major Histocompatibility Complex) presenting an antigen(foreign peptide) to the T cell receptor.
What is The bond that links two amino acids called?
This is called a peptide bond, or peptide linkage.
Is exponential signal an energy signal or power signal?
If the signal is not bounded by a step function, then an exponential signal is neither a power nor an energy signal. So the answer is neither.
Is impulse function is an energy signal or a power signal or both Explain?
it can not be both!
How might placing a peptide into a non-polar solution affect the tertiary structure of the peptide?
Placing a peptide into a non-polar solution can disrupt its tertiary structure, as non-polar solvents can disrupt hydrogen bonding and hydrophobic interactions that stabilize the structure. This disruption can lead to the unfolding or denaturation of the peptide, altering its overall shape and function.
What peptide codes for?
Peptides are short chains of amino acids that are typically produced through the translation of specific genes. Each peptide corresponds to a sequence of nucleotides in DNA or RNA, with the genetic code determining the order of amino acids in the peptide. These sequences can have various functions, including acting as hormones, neurotransmitters, or components of proteins that perform structural or enzymatic roles in the body. Thus, the specific peptide code dictates the biological activity and function of the resulting peptide.
