The process of protein synthesis and secretion starts from the endoplasmic reticulum. The
polypeptide chain is formed in the ribosomes, and then transferred to the Golgi apparatus, where
the final modifications are done. The Golgi apparatus sorts the modified poly peptide molecules
and packages into new transport vesicles which reach their particular destinations. The
tranlocons transport the polypeptides with a signal sequence to the interior of the endoplasmic
reticulum. Multiple control mechanisms of the endoplasmic reticulum ensures that only properly
folded proteins to export towards the Golgi apparatus.
The plasma membrane proteins synthesized in the endoplasmic reticulum (ER). The proteins
generally contain endoplasmic reticulum signal sequence at their N-terminus, which directs them
to the rough endoplasmic reticulum. After completion of translation process in the RER, the
polypeptide chains get inserted into the ER membrane or into the lumen of ER.
Some proteins move to the transport vesicles, which fuse together to form cis- Golgi vesicles, the
cis-form again moves to trans-form. During this process, many proteins undergo modifications
particularly at oligosaccharide chains. From the trans-Golgi vesicles, proteins move to cell
membrane through small transportation vesicles (exocytosis).
Solution
The process of protein synthesis and secretion starts from the endoplasmic reticulum. The
polypeptide chain is formed in the ribosomes, and then transferred to the Golgi apparatus, where
the final modifications are done. The Golgi apparatus sorts the modified poly peptide molecules
and packages into new transport vesicles which reach their particular destinations. The
tranlocons transport the polypeptides with a signal sequence to the interior of the endoplasmic
reticulum. Multiple control mechanisms of the endoplasmic reticulum ensures that only properly
folded proteins to export towards the Golgi apparatus.
The plasma membrane proteins synthesized in the endoplasmic reticulum (ER). The proteins
generally contain endoplasmic reticulum signal sequence at their N-terminus, which directs them
to the rough endoplasmic reticulum. After completion of translation process in the RER, the
polypeptide chains get inserted into the ER membrane or into the lumen of ER.
Some proteins move to the transport vesicles, which fuse together to form cis- Golgi vesicles, the
cis-form again moves to trans-form. During this process, many proteins undergo modifications
particularly at oligosaccharide chains. From the trans-Golgi vesicles, proteins move to cell
membrane through small transportation vesicles (exocytosis)..
Describe the role signal sequences play in protein localization. NES.pdffippsximenaal85949
Describe the role signal sequences play in protein localization. NES, NJS, Stop start, ER signal
sequences Describe the process of events involved in ligand production to exocytosis.
PowerPointslide 6 plus written details Post transcriptional modifications. Discuss 5\'capping,
splicing, poly A tail Describe three different mechanisms of signal termination Inhibitors -
extracellular, receptor inhibitors, internalization phosphorylation/dephosphorylation Give an
account of the role vesicle tethering plays in endocytosis. SNARES V and T, Rab effectors,
tethering docking fusion Protein glycosylation, discuss, its importance and the process of
glycosylation Occurs in ER, modified in Golgi, etc... Autocrine, paracrine and endocrine.
Discuss the differences between these signaling mechanisms. Write an account how signaling
can be terminated at the level of receptors Different cells can react differently to the same signal.
Discuss Example acetylcholine Outline the process of plasma membrane receptor production to
its final destination Two major populations of ribosome exist in our cells. Discuss
Solution
Ques-1:
The role of signal seqeunecs in protein localization:
ER signal sequences and stop-start:
Signal peptidase normally localized in the “endoplasmic reticulum” of eukaryotic cell. These
serine proteases digest the “nascent secretory polypeptides” after translation & post & co-
translational modifications. These signal peptidase enzymes are going to cleave signal peptides
of membrane proteins at their N-terminals.
Signal sequence of \"6 to 10 amino acid length\" normally cleaved by signal peptidases during or
after completion of translocation from ribosome & before entering into the endoplasmic
reticulum
Cotranslational translocation is mediated by signal recognition particle (SRP) & it is a 11S
ribonucleoprotien essential for translocation of nascent polypeptide to the “ER lumen”. This SRP
is formed of a nucleoprotein with 7S RNA, 11S & combines with several proteins to form the
eukaryotic signal recognition particle. The nascent polypeptide is emerged from the ribosomes,
followed by “recognition of signal sequence & bound by signal recognition particle(SRP), a
hydrophobic residue with 6 polypeptides 7SL RNA.
Therefore, when this SRP sequence exits from the ribosome, the nascent polypeptide stops being
translocated into the ER lumen. Signal recognition particle has bound by a signal sequence and
flowed by slow protein synthesis in the translation. This SRP further is going to bind to the
location near by endoplasmic reticulum followed by release of signal recognition particle but the
growing polypeptide is in the form of protein-ribosome complex that is at the exact location for
further protein translocation through Golgi-vesicle translocation channel.
The nuclear localization signal sequence (NLS) is mainly associated with “tags” in which amino
acids or proteins are imported into the nucleus using Ran-GTPases activity by nuclear transport.
So .
Describe the similarities and differences (3 or 4 complete sentences.pdfpearlcoburnsanche303
Describe the similarities and differences (3 or 4 complete sentences) in the synthesis “pathway”
(i.e. all the organelles and cellular components involved) between a protein that is NOT secreted
(i.e., functions within the cytoplasm) versus a protein that IS secreted
Solution
The process of protein synthesis and secretion starts from the endoplasmic reticulum. The
polypeptide chain is formed in the ribosomes, and then transferred to the Golgi apparatus, where
the final modifications are done. The Golgi apparatus sorts the modified poly peptide molecules
and packages into new transport vesicles which reach their particular destinations.
The proteins that are intended to be used within the cell (intracellular proteins) are produced by
the ribosomes that float freely in the cytoplasm.
The proteins that are intended to be secreted out of the cell are synthesized by the ribosomes of
the RER. This system contains “cisternae.” They are the fluid filled sacs, into which the
synthesized proteins are released.
They modify these proteins by different processes. The proteins generally contain endoplasmic
reticulum signal sequence at their N-terminus, which directs them to the rough endoplasmic
reticulum. They enter into the endoplasmic reticulum as the lipid end of the protein (first 30
amino acids are hydrophobic) is attracted by the lipid component of the endoplasmic reticulum.
Once they are in the ER, the hydrophobic chain is removed by the enzymatic process. The
secretory proteins are transported to the Golgi apparatus for further modification. From the trans-
Golgi vesicles, proteins move to cell membrane through small transportation vesicles
(exocytosis). Some of then may be degraded by lysosomes as a part of regulation of gene
expression..
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
Describe the role signal sequences play in protein localization. NES.pdffippsximenaal85949
Describe the role signal sequences play in protein localization. NES, NJS, Stop start, ER signal
sequences Describe the process of events involved in ligand production to exocytosis.
PowerPointslide 6 plus written details Post transcriptional modifications. Discuss 5\'capping,
splicing, poly A tail Describe three different mechanisms of signal termination Inhibitors -
extracellular, receptor inhibitors, internalization phosphorylation/dephosphorylation Give an
account of the role vesicle tethering plays in endocytosis. SNARES V and T, Rab effectors,
tethering docking fusion Protein glycosylation, discuss, its importance and the process of
glycosylation Occurs in ER, modified in Golgi, etc... Autocrine, paracrine and endocrine.
Discuss the differences between these signaling mechanisms. Write an account how signaling
can be terminated at the level of receptors Different cells can react differently to the same signal.
Discuss Example acetylcholine Outline the process of plasma membrane receptor production to
its final destination Two major populations of ribosome exist in our cells. Discuss
Solution
Ques-1:
The role of signal seqeunecs in protein localization:
ER signal sequences and stop-start:
Signal peptidase normally localized in the “endoplasmic reticulum” of eukaryotic cell. These
serine proteases digest the “nascent secretory polypeptides” after translation & post & co-
translational modifications. These signal peptidase enzymes are going to cleave signal peptides
of membrane proteins at their N-terminals.
Signal sequence of \"6 to 10 amino acid length\" normally cleaved by signal peptidases during or
after completion of translocation from ribosome & before entering into the endoplasmic
reticulum
Cotranslational translocation is mediated by signal recognition particle (SRP) & it is a 11S
ribonucleoprotien essential for translocation of nascent polypeptide to the “ER lumen”. This SRP
is formed of a nucleoprotein with 7S RNA, 11S & combines with several proteins to form the
eukaryotic signal recognition particle. The nascent polypeptide is emerged from the ribosomes,
followed by “recognition of signal sequence & bound by signal recognition particle(SRP), a
hydrophobic residue with 6 polypeptides 7SL RNA.
Therefore, when this SRP sequence exits from the ribosome, the nascent polypeptide stops being
translocated into the ER lumen. Signal recognition particle has bound by a signal sequence and
flowed by slow protein synthesis in the translation. This SRP further is going to bind to the
location near by endoplasmic reticulum followed by release of signal recognition particle but the
growing polypeptide is in the form of protein-ribosome complex that is at the exact location for
further protein translocation through Golgi-vesicle translocation channel.
The nuclear localization signal sequence (NLS) is mainly associated with “tags” in which amino
acids or proteins are imported into the nucleus using Ran-GTPases activity by nuclear transport.
So .
Describe the similarities and differences (3 or 4 complete sentences.pdfpearlcoburnsanche303
Describe the similarities and differences (3 or 4 complete sentences) in the synthesis “pathway”
(i.e. all the organelles and cellular components involved) between a protein that is NOT secreted
(i.e., functions within the cytoplasm) versus a protein that IS secreted
Solution
The process of protein synthesis and secretion starts from the endoplasmic reticulum. The
polypeptide chain is formed in the ribosomes, and then transferred to the Golgi apparatus, where
the final modifications are done. The Golgi apparatus sorts the modified poly peptide molecules
and packages into new transport vesicles which reach their particular destinations.
The proteins that are intended to be used within the cell (intracellular proteins) are produced by
the ribosomes that float freely in the cytoplasm.
The proteins that are intended to be secreted out of the cell are synthesized by the ribosomes of
the RER. This system contains “cisternae.” They are the fluid filled sacs, into which the
synthesized proteins are released.
They modify these proteins by different processes. The proteins generally contain endoplasmic
reticulum signal sequence at their N-terminus, which directs them to the rough endoplasmic
reticulum. They enter into the endoplasmic reticulum as the lipid end of the protein (first 30
amino acids are hydrophobic) is attracted by the lipid component of the endoplasmic reticulum.
Once they are in the ER, the hydrophobic chain is removed by the enzymatic process. The
secretory proteins are transported to the Golgi apparatus for further modification. From the trans-
Golgi vesicles, proteins move to cell membrane through small transportation vesicles
(exocytosis). Some of then may be degraded by lysosomes as a part of regulation of gene
expression..
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
Proteins destined for secretion, integration in the plasma membrane, or inclusion in lysosomes generally share pathway that begins in the endoplasmic reticulum. Proteins destined for mitochondria, chloroplasts, or the nucleus use three separate mechanisms. And proteins destined for the cytosol simply remain where they are synthesized.
Introduction
Protein synthesis
Synthesis of secretory proteins on membrane-bound ribosomes
Processing of newly synthesized proteins in the ER
Synthesis of integral membrane protein on membrane bound ribosomes
Maintenance of membrane asymmetry
Conclusion
Reference
The main organelles in protein sorting and targeting are Rough endop.pdfanushasarees
The main organelles in protein sorting and targeting are Rough endoplasmic reticulum. As the
question is all about sorting and targeting to membrane and secretion, I will stick to only these
two targeting pathways. Please note the mechansm of targeting proteins to other organelles such
as mitichondria, ER, chloroplast is different.
Journey of a secretory protein:
The protein sorting and targeting occur in endoplasmic reticulum. Most of the secretory proteins
as well as membrane proteins are translocated into ER co-translationally (Co-translational
translocation). i.e, they are moved into ER while their translation is going on. this translocation
process is mediated by Signal recognition particle (SRP). SRP recognizes N-terminal signal
peptide on the protein that is being translated. The translation process pauses for a while when
the ribosome-protein-SRP complex is being transported to SRP receptor on the ER membrane.
The protein is inserted into translocon channel on ER membrane and enters ER. The signaal
sequence from nascent peptide is immediately cleaved in case of secretoey proteins and type I
transmembrane proteins by signal peptidase. the translation resumes directing the protein being
formed into ER. Inside the ER, chaperone proteins bind the protein to guide through correct
folding. Then the protein is transported by ER membrane vesicles to golgi apparatus for further
processing like protein modification and glycosylation. ER--- cis-golgi---trans---golgi---
lysosomes. the proteins from lysosomes fuse with membrane and according to the signals present
in nascent proteins, they either remain as transmembrane proteins or secreted out of the
membrane.
transmembrane G-receptors span the membrane seven times (also called serpentine receptors)
donot contain signal sequence at N-terminal. The first transmembrane domain acts as the signal
sequence that is recognized by SRP.
Some secretory proteins as well as transmembrane proteins may undero post-translational
translocation. i.e, transportation to ER after the completion of protein synthesis. the entire
process is believed to be same as co-translational translocation.
Solution
The main organelles in protein sorting and targeting are Rough endoplasmic reticulum. As the
question is all about sorting and targeting to membrane and secretion, I will stick to only these
two targeting pathways. Please note the mechansm of targeting proteins to other organelles such
as mitichondria, ER, chloroplast is different.
Journey of a secretory protein:
The protein sorting and targeting occur in endoplasmic reticulum. Most of the secretory proteins
as well as membrane proteins are translocated into ER co-translationally (Co-translational
translocation). i.e, they are moved into ER while their translation is going on. this translocation
process is mediated by Signal recognition particle (SRP). SRP recognizes N-terminal signal
peptide on the protein that is being translated. The translation process pauses for a .
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
#includestdio.h#includestdlib.h structure of a stack node .pdfankitcomputer11
#include
#include
/* structure of a stack node */
struct sNode
{
int data;
struct sNode *next;
};
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data);
/* Function to pop an item from stack*/
int pop(struct sNode** top_ref);
/* structure of queue having two stacks */
struct queue
{
struct sNode *stack1;
struct sNode *stack2;
};
/* Function to enqueue an item to queue */
void enQueue(struct queue *q, int x)
{
push(&q->stack1, x);
}
/* Function to dequeue an item from queue */
int deQueue(struct queue *q)
{
int x;
/* If both stacks are empty then error */
if(q->stack1 == NULL && q->stack2 == NULL)
{
printf(\"Q is empty\");
getchar();
exit(0);
}
/* Move elements from satck1 to stack 2 only if
stack2 is empty */
if(q->stack2 == NULL)
{
while(q->stack1 != NULL)
{
x = pop(&q->stack1);
push(&q->stack2, x);
}
}
x = pop(&q->stack2);
return x;
}
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data)
{
/* allocate node */
struct sNode* new_node =
(struct sNode*) malloc(sizeof(struct sNode));
if(new_node == NULL)
{
printf(\"Stack overflow \ \");
getchar();
exit(0);
}
/* put in the data */
new_node->data = new_data;
/* link the old list off the new node */
new_node->next = (*top_ref);
/* move the head to point to the new node */
(*top_ref) = new_node;
}
/* Function to pop an item from stack*/
int pop(struct sNode** top_ref)
{
int res;
struct sNode *top;
/*If stack is empty then error */
if(*top_ref == NULL)
{
printf(\"Stack overflow \ \");
getchar();
exit(0);
}
else
{
top = *top_ref;
res = top->data;
*top_ref = top->next;
free(top);
return res;
}
}
/* Driver function to test anove functions */
int main()
{
/* Create a queue with items 1 2 3*/
struct queue *q = (struct queue*)malloc(sizeof(struct queue));
q->stack1 = NULL;
q->stack2 = NULL;
enQueue(q, 1);
enQueue(q, 2);
enQueue(q, 3);
/* Dequeue items */
printf(\"%d \", deQueue(q));
printf(\"%d \", deQueue(q));
printf(\"%d \", deQueue(q));
getchar();
}
Solution
#include
#include
/* structure of a stack node */
struct sNode
{
int data;
struct sNode *next;
};
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data);
/* Function to pop an item from stack*/
int pop(struct sNode** top_ref);
/* structure of queue having two stacks */
struct queue
{
struct sNode *stack1;
struct sNode *stack2;
};
/* Function to enqueue an item to queue */
void enQueue(struct queue *q, int x)
{
push(&q->stack1, x);
}
/* Function to dequeue an item from queue */
int deQueue(struct queue *q)
{
int x;
/* If both stacks are empty then error */
if(q->stack1 == NULL && q->stack2 == NULL)
{
printf(\"Q is empty\");
getchar();
exit(0);
}
/* Move elements from satck1 to stack 2 only if
stack2 is empty */
if(q->stack2 == NULL)
{
while(q->stack1 != NULL)
{
x = pop(&q->stack1);
push(&q->stack2, x);
}
}
x = pop(&q->stack2);
return x;
}
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data)
{
/* allocate node */
struct s.
Solution Since we know that the subshell with .pdfankitcomputer11
Solution
: Since we know that the subshell with : n=2 and l=1 is the 2p subshell; Similarly : if n=3 and
l=0, it is the 3s subshell and so on that\'s why it is n=3, l=2 and m_l=0 Please rate.
More Related Content
Similar to The process of protein synthesis and secretion starts from the endop.pdf
Introduction
Protein synthesis
Synthesis of secretory proteins on membrane-bound ribosomes
Processing of newly synthesized proteins in the ER
Synthesis of integral membrane protein on membrane bound ribosomes
Maintenance of membrane asymmetry
Conclusion
Reference
The main organelles in protein sorting and targeting are Rough endop.pdfanushasarees
The main organelles in protein sorting and targeting are Rough endoplasmic reticulum. As the
question is all about sorting and targeting to membrane and secretion, I will stick to only these
two targeting pathways. Please note the mechansm of targeting proteins to other organelles such
as mitichondria, ER, chloroplast is different.
Journey of a secretory protein:
The protein sorting and targeting occur in endoplasmic reticulum. Most of the secretory proteins
as well as membrane proteins are translocated into ER co-translationally (Co-translational
translocation). i.e, they are moved into ER while their translation is going on. this translocation
process is mediated by Signal recognition particle (SRP). SRP recognizes N-terminal signal
peptide on the protein that is being translated. The translation process pauses for a while when
the ribosome-protein-SRP complex is being transported to SRP receptor on the ER membrane.
The protein is inserted into translocon channel on ER membrane and enters ER. The signaal
sequence from nascent peptide is immediately cleaved in case of secretoey proteins and type I
transmembrane proteins by signal peptidase. the translation resumes directing the protein being
formed into ER. Inside the ER, chaperone proteins bind the protein to guide through correct
folding. Then the protein is transported by ER membrane vesicles to golgi apparatus for further
processing like protein modification and glycosylation. ER--- cis-golgi---trans---golgi---
lysosomes. the proteins from lysosomes fuse with membrane and according to the signals present
in nascent proteins, they either remain as transmembrane proteins or secreted out of the
membrane.
transmembrane G-receptors span the membrane seven times (also called serpentine receptors)
donot contain signal sequence at N-terminal. The first transmembrane domain acts as the signal
sequence that is recognized by SRP.
Some secretory proteins as well as transmembrane proteins may undero post-translational
translocation. i.e, transportation to ER after the completion of protein synthesis. the entire
process is believed to be same as co-translational translocation.
Solution
The main organelles in protein sorting and targeting are Rough endoplasmic reticulum. As the
question is all about sorting and targeting to membrane and secretion, I will stick to only these
two targeting pathways. Please note the mechansm of targeting proteins to other organelles such
as mitichondria, ER, chloroplast is different.
Journey of a secretory protein:
The protein sorting and targeting occur in endoplasmic reticulum. Most of the secretory proteins
as well as membrane proteins are translocated into ER co-translationally (Co-translational
translocation). i.e, they are moved into ER while their translation is going on. this translocation
process is mediated by Signal recognition particle (SRP). SRP recognizes N-terminal signal
peptide on the protein that is being translated. The translation process pauses for a .
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations in the cell or outside it. Proteins can be targeted to the inner space of an organelle, different intracellular membranes, plasma membrane, or to exterior of the cell via secretion.
#includestdio.h#includestdlib.h structure of a stack node .pdfankitcomputer11
#include
#include
/* structure of a stack node */
struct sNode
{
int data;
struct sNode *next;
};
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data);
/* Function to pop an item from stack*/
int pop(struct sNode** top_ref);
/* structure of queue having two stacks */
struct queue
{
struct sNode *stack1;
struct sNode *stack2;
};
/* Function to enqueue an item to queue */
void enQueue(struct queue *q, int x)
{
push(&q->stack1, x);
}
/* Function to dequeue an item from queue */
int deQueue(struct queue *q)
{
int x;
/* If both stacks are empty then error */
if(q->stack1 == NULL && q->stack2 == NULL)
{
printf(\"Q is empty\");
getchar();
exit(0);
}
/* Move elements from satck1 to stack 2 only if
stack2 is empty */
if(q->stack2 == NULL)
{
while(q->stack1 != NULL)
{
x = pop(&q->stack1);
push(&q->stack2, x);
}
}
x = pop(&q->stack2);
return x;
}
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data)
{
/* allocate node */
struct sNode* new_node =
(struct sNode*) malloc(sizeof(struct sNode));
if(new_node == NULL)
{
printf(\"Stack overflow \ \");
getchar();
exit(0);
}
/* put in the data */
new_node->data = new_data;
/* link the old list off the new node */
new_node->next = (*top_ref);
/* move the head to point to the new node */
(*top_ref) = new_node;
}
/* Function to pop an item from stack*/
int pop(struct sNode** top_ref)
{
int res;
struct sNode *top;
/*If stack is empty then error */
if(*top_ref == NULL)
{
printf(\"Stack overflow \ \");
getchar();
exit(0);
}
else
{
top = *top_ref;
res = top->data;
*top_ref = top->next;
free(top);
return res;
}
}
/* Driver function to test anove functions */
int main()
{
/* Create a queue with items 1 2 3*/
struct queue *q = (struct queue*)malloc(sizeof(struct queue));
q->stack1 = NULL;
q->stack2 = NULL;
enQueue(q, 1);
enQueue(q, 2);
enQueue(q, 3);
/* Dequeue items */
printf(\"%d \", deQueue(q));
printf(\"%d \", deQueue(q));
printf(\"%d \", deQueue(q));
getchar();
}
Solution
#include
#include
/* structure of a stack node */
struct sNode
{
int data;
struct sNode *next;
};
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data);
/* Function to pop an item from stack*/
int pop(struct sNode** top_ref);
/* structure of queue having two stacks */
struct queue
{
struct sNode *stack1;
struct sNode *stack2;
};
/* Function to enqueue an item to queue */
void enQueue(struct queue *q, int x)
{
push(&q->stack1, x);
}
/* Function to dequeue an item from queue */
int deQueue(struct queue *q)
{
int x;
/* If both stacks are empty then error */
if(q->stack1 == NULL && q->stack2 == NULL)
{
printf(\"Q is empty\");
getchar();
exit(0);
}
/* Move elements from satck1 to stack 2 only if
stack2 is empty */
if(q->stack2 == NULL)
{
while(q->stack1 != NULL)
{
x = pop(&q->stack1);
push(&q->stack2, x);
}
}
x = pop(&q->stack2);
return x;
}
/* Function to push an item to stack*/
void push(struct sNode** top_ref, int new_data)
{
/* allocate node */
struct s.
Solution Since we know that the subshell with .pdfankitcomputer11
Solution
: Since we know that the subshell with : n=2 and l=1 is the 2p subshell; Similarly : if n=3 and
l=0, it is the 3s subshell and so on that\'s why it is n=3, l=2 and m_l=0 Please rate.
let V be nonempty open subset of X then V inters.pdfankitcomputer11
let V be nonempty open subset of X then V intersection U is nonempty because U
is dense in X therefore V is not contained in X/U so X/U is nowhere dense in X
Solution
let V be nonempty open subset of X then V intersection U is nonempty because U
is dense in X therefore V is not contained in X/U so X/U is nowhere dense in X.
Look at the periodic table. When Be loses its f.pdfankitcomputer11
Look at the periodic table. When Be loses it\'s first electron it now only has 3
electroms (Just like Li) when it loses it\'s second electron in only has 2 electrons (just like He)
when it loses it\'s third electron it goes from 1s2 to 1s1 therefore the 1s orbital loses an electron
in the third ionization step for Be
Solution
Look at the periodic table. When Be loses it\'s first electron it now only has 3
electroms (Just like Li) when it loses it\'s second electron in only has 2 electrons (just like He)
when it loses it\'s third electron it goes from 1s2 to 1s1 therefore the 1s orbital loses an electron
in the third ionization step for Be.
taking L.T.,,,,,,,,,,,,Y(s)[s^2+4s+14]=L(T(t))...........for periodic functions the trans
form is given as ........inte(0 to T)(T(t))exp(-st)*dt/[1-exp(-sT)].........solving we get the the
integral as [(1+exp(-s)-2*exp(-s/2)/s^2.+ (exp(-s)-exp(-s/2))/s]...........putting it in the equation
we get [(1+exp(-s)-2*exp(-s/2)/s^2.+ (exp(-s)-exp(-s/2))/s]/([s^2+4s+14])
Solution
taking L.T.,,,,,,,,,,,,Y(s)[s^2+4s+14]=L(T(t))...........for periodic functions the trans
form is given as ........inte(0 to T)(T(t))exp(-st)*dt/[1-exp(-sT)].........solving we get the the
integral as [(1+exp(-s)-2*exp(-s/2)/s^2.+ (exp(-s)-exp(-s/2))/s]...........putting it in the equation
we get [(1+exp(-s)-2*exp(-s/2)/s^2.+ (exp(-s)-exp(-s/2))/s]/([s^2+4s+14]).
the salt is neutral in charge. OS of Ca is +2, so.pdfankitcomputer11
the salt is neutral in charge. OS of Ca is +2, so (NO3)2 bears -2 charges, so NO3
bears -1 charge, we know O holds -2 charge Thus, (the charge of N) + -2x3 =-1 so, N = +5 Ca
+2, N +5, O -2
Solution
the salt is neutral in charge. OS of Ca is +2, so (NO3)2 bears -2 charges, so NO3
bears -1 charge, we know O holds -2 charge Thus, (the charge of N) + -2x3 =-1 so, N = +5 Ca
+2, N +5, O -2.
nonmetals, metals, metalloids, and gases. They ar.pdfankitcomputer11
nonmetals, metals, metalloids, and gases. They are important because they are
involved in everyday life
Solution
nonmetals, metals, metalloids, and gases. They are important because they are
involved in everyday life.
In thermodynamics, a state function, function of .pdfankitcomputer11
In thermodynamics, a state function, function of state, state quantity, or state
variable is a property of a system that depends only on the current state of the system, not on the
way in which the system acquired that state (independent of path). A state function describes the
equilibrium state of a system. For example, internal energy, enthalpy, and entropy are state
quantities because they describe quantitatively an equilibrium state of a thermodynamic system,
irrespective of how the system arrived in that state. In contrast, mechanical work and heat are
process quantities because their values depend on the specific transition (or path) between two
equilibrium states. The following are considered to be state functions in thermodynamics: Mass
(m) Energy (E) Enthalpy (H) Internal energy (U) Gibbs free energy (G) Helmholtz free energy
(A) Exergy Entropy (S) Pressure (p) Temperature (T) Volume (V) Chemical composition
Specific volume (v) or its reciprocal Density (?) Fugacity Altitude Particle number (ni)
Solution
In thermodynamics, a state function, function of state, state quantity, or state
variable is a property of a system that depends only on the current state of the system, not on the
way in which the system acquired that state (independent of path). A state function describes the
equilibrium state of a system. For example, internal energy, enthalpy, and entropy are state
quantities because they describe quantitatively an equilibrium state of a thermodynamic system,
irrespective of how the system arrived in that state. In contrast, mechanical work and heat are
process quantities because their values depend on the specific transition (or path) between two
equilibrium states. The following are considered to be state functions in thermodynamics: Mass
(m) Energy (E) Enthalpy (H) Internal energy (U) Gibbs free energy (G) Helmholtz free energy
(A) Exergy Entropy (S) Pressure (p) Temperature (T) Volume (V) Chemical composition
Specific volume (v) or its reciprocal Density (?) Fugacity Altitude Particle number (ni).
The IUPAC names of the given compounds is 2-chloro-1-butanol.pdfankitcomputer11
The IUPAC names of the given compounds is:
2-chloro-1-butanol
2-methoxycyclohexanol
Solution
The IUPAC names of the given compounds is:
2-chloro-1-butanol
2-methoxycyclohexanol.
Solution - (c) - 20001 SharesCalculation of Number of shares to be.pdfankitcomputer11
Solution
- (c) - 20001 Shares
Calculation of Number of shares to be controlled to guarantee the election to be board.
= [1/(Number of Seats of Board of Directors + 1)*Shares Outstanding] + 1
= [1/(5+1)*120000 + 1]
= [(1/6)*120000] + 1
= 20001 Shares..
Move decimal to behind the first number4.71Round4.714.71 X 1.pdfankitcomputer11
Move decimal to behind the first number
4.71
Round
4.71
4.71 X 10^2 (2=the number of spaces you had to move the decimal)
Solution
Move decimal to behind the first number
4.71
Round
4.71
4.71 X 10^2 (2=the number of spaces you had to move the decimal).
Lewis acid is the electron pair acceptorLewis base is the electron.pdfankitcomputer11
Lewis acid is the electron pair acceptor
Lewis base is the electron pair donar
a) OH- + Al(OH)3 -----> Al(OH)4-
Al(OH)3 is the lewis acid
OH- is the lewis base
b) SO3 + H2O --------> H2SO4
H2O is the lewis acid
SO3 is the lewis base
H2O is the lewis acid
SO3 is the lewis base
c) Co3+ + 6NH3 -----> Co(NH3)63+
Co 3+ is the lewis acid
NH3 is the lewis base
Co 3+ is the lewis acid
NH3 is the lewis base
Solution
Lewis acid is the electron pair acceptor
Lewis base is the electron pair donar
a) OH- + Al(OH)3 -----> Al(OH)4-
Al(OH)3 is the lewis acid
OH- is the lewis base
b) SO3 + H2O --------> H2SO4
H2O is the lewis acid
SO3 is the lewis base
H2O is the lewis acid
SO3 is the lewis base
c) Co3+ + 6NH3 -----> Co(NH3)63+
Co 3+ is the lewis acid
NH3 is the lewis base
Co 3+ is the lewis acid
NH3 is the lewis base.
first treat with alcoholic KOH to get cyclo hexene and then treat it.pdfankitcomputer11
first treat with alcoholic KOH to get cyclo hexene and then treat it with alkaline KMnO4 to get
trans cyclohxane -1,2 -diol
Solution
first treat with alcoholic KOH to get cyclo hexene and then treat it with alkaline KMnO4 to get
trans cyclohxane -1,2 -diol.
An azeotrope is a mixture of two or more liquids .pdfankitcomputer11
An azeotrope is a mixture of two or more liquids in such a ratio that its composition
cannot be changed by simple distillation. This occurs because, when an azeotrope is boiled, the
resulting vapor has the same ratio of constituents as the original mixture. Because their
composition is unchanged by distillation, azeotropes are also called constant boiling mixtures.
Common drying agenets for organic compounds : Alcohols : Anhydrous K2CO3, CaSO4 or
Mg2SO4 and CaO Alkylhalides/aryl halides : Anhydrous CaCl2,CaSO4 or Mg2SO4 and
phosphoric acid Saturated aromatic hydrocarbonds : CaCl2,CaSO4 and phosphoric oxide
Aldehydes : CaSO4,Mg2SO4 Na2SO4 Ketones : CaSO4,MgSO4 ,NaSO4 or K2CO3 Organic
bases : Solid KOH/NaOH ,CaO or Barium oxide Organic acids : Calcium sulphate, Mg2SO4
Solution
An azeotrope is a mixture of two or more liquids in such a ratio that its composition
cannot be changed by simple distillation. This occurs because, when an azeotrope is boiled, the
resulting vapor has the same ratio of constituents as the original mixture. Because their
composition is unchanged by distillation, azeotropes are also called constant boiling mixtures.
Common drying agenets for organic compounds : Alcohols : Anhydrous K2CO3, CaSO4 or
Mg2SO4 and CaO Alkylhalides/aryl halides : Anhydrous CaCl2,CaSO4 or Mg2SO4 and
phosphoric acid Saturated aromatic hydrocarbonds : CaCl2,CaSO4 and phosphoric oxide
Aldehydes : CaSO4,Mg2SO4 Na2SO4 Ketones : CaSO4,MgSO4 ,NaSO4 or K2CO3 Organic
bases : Solid KOH/NaOH ,CaO or Barium oxide Organic acids : Calcium sulphate, Mg2SO4.
Here we have sodium bisulfate NaHSO4, as you have shown the ions pr.pdfankitcomputer11
Here we have sodium bisulfate: NaHSO4, as you have shown the ions present are of equal
charge. Thus, there are equal amounts of both ions.
Recall molarity,
molarity = mole / volume
Thus, we can calculate the number of moles:
M = mol / V
0.55 = mol / 1.32L
Solving for moles gives: mole = 0.726 moles.
Since we established earlier, both species (Na+ and HSO4- are present in equal amounts), thus
moles (Na+) = moles (HSO4-) = 0.726 moles
Please don\'t forget to rate, I hope this helped! :)
Solution
Here we have sodium bisulfate: NaHSO4, as you have shown the ions present are of equal
charge. Thus, there are equal amounts of both ions.
Recall molarity,
molarity = mole / volume
Thus, we can calculate the number of moles:
M = mol / V
0.55 = mol / 1.32L
Solving for moles gives: mole = 0.726 moles.
Since we established earlier, both species (Na+ and HSO4- are present in equal amounts), thus
moles (Na+) = moles (HSO4-) = 0.726 moles
Please don\'t forget to rate, I hope this helped! :).
Frontal lobe is the region of forebrain which comprises of various c.pdfankitcomputer11
Frontal lobe is the region of forebrain which comprises of various centres for motor and concious
functions, including intelligence and decision making. Some specific areas are defined in the
frontal lobe according to their specifc functions. These are:
1. The motor strip: It is a part of the primary motor cortex of the frontal and prefrontal cortex of
the brain and maintains essential functions related to motion and movement. It is also known as
the precentral gyrus.
2. The precentral gyrus: This area structurally forms the posterior lobes of the frontal area cortex
and is important for the activity of motor neurons of limbs.
3. Broca\'s speech area: This region resides in a major part of the frontal lobe and is essential for
learning ability of languages and speech.
Importantly, Wernicke\'s speech area is an integral part of the temporal lobe of the brain near the
ears. It is not a part of the frontal lobe. Thus, the correct answers is choice A, WERNICKE\'S
SPEECH AREA.
Solution
Frontal lobe is the region of forebrain which comprises of various centres for motor and concious
functions, including intelligence and decision making. Some specific areas are defined in the
frontal lobe according to their specifc functions. These are:
1. The motor strip: It is a part of the primary motor cortex of the frontal and prefrontal cortex of
the brain and maintains essential functions related to motion and movement. It is also known as
the precentral gyrus.
2. The precentral gyrus: This area structurally forms the posterior lobes of the frontal area cortex
and is important for the activity of motor neurons of limbs.
3. Broca\'s speech area: This region resides in a major part of the frontal lobe and is essential for
learning ability of languages and speech.
Importantly, Wernicke\'s speech area is an integral part of the temporal lobe of the brain near the
ears. It is not a part of the frontal lobe. Thus, the correct answers is choice A, WERNICKE\'S
SPEECH AREA..
The French Revolution, which began in 1789, was a period of radical social and political upheaval in France. It marked the decline of absolute monarchies, the rise of secular and democratic republics, and the eventual rise of Napoleon Bonaparte. This revolutionary period is crucial in understanding the transition from feudalism to modernity in Europe.
For more information, visit-www.vavaclasses.com
Operation “Blue Star” is the only event in the history of Independent India where the state went into war with its own people. Even after about 40 years it is not clear if it was culmination of states anger over people of the region, a political game of power or start of dictatorial chapter in the democratic setup.
The people of Punjab felt alienated from main stream due to denial of their just demands during a long democratic struggle since independence. As it happen all over the word, it led to militant struggle with great loss of lives of military, police and civilian personnel. Killing of Indira Gandhi and massacre of innocent Sikhs in Delhi and other India cities was also associated with this movement.
Acetabularia Information For Class 9 .docxvaibhavrinwa19
Acetabularia acetabulum is a single-celled green alga that in its vegetative state is morphologically differentiated into a basal rhizoid and an axially elongated stalk, which bears whorls of branching hairs. The single diploid nucleus resides in the rhizoid.
Unit 8 - Information and Communication Technology (Paper I).pdfThiyagu K
This slides describes the basic concepts of ICT, basics of Email, Emerging Technology and Digital Initiatives in Education. This presentations aligns with the UGC Paper I syllabus.
Normal Labour/ Stages of Labour/ Mechanism of LabourWasim Ak
Normal labor is also termed spontaneous labor, defined as the natural physiological process through which the fetus, placenta, and membranes are expelled from the uterus through the birth canal at term (37 to 42 weeks
Francesca Gottschalk - How can education support child empowerment.pptxEduSkills OECD
Francesca Gottschalk from the OECD’s Centre for Educational Research and Innovation presents at the Ask an Expert Webinar: How can education support child empowerment?
How to Make a Field invisible in Odoo 17Celine George
It is possible to hide or invisible some fields in odoo. Commonly using “invisible” attribute in the field definition to invisible the fields. This slide will show how to make a field invisible in odoo 17.
Welcome to TechSoup New Member Orientation and Q&A (May 2024).pdfTechSoup
In this webinar you will learn how your organization can access TechSoup's wide variety of product discount and donation programs. From hardware to software, we'll give you a tour of the tools available to help your nonprofit with productivity, collaboration, financial management, donor tracking, security, and more.
Welcome to TechSoup New Member Orientation and Q&A (May 2024).pdf
The process of protein synthesis and secretion starts from the endop.pdf
1. The process of protein synthesis and secretion starts from the endoplasmic reticulum. The
polypeptide chain is formed in the ribosomes, and then transferred to the Golgi apparatus, where
the final modifications are done. The Golgi apparatus sorts the modified poly peptide molecules
and packages into new transport vesicles which reach their particular destinations. The
tranlocons transport the polypeptides with a signal sequence to the interior of the endoplasmic
reticulum. Multiple control mechanisms of the endoplasmic reticulum ensures that only properly
folded proteins to export towards the Golgi apparatus.
The plasma membrane proteins synthesized in the endoplasmic reticulum (ER). The proteins
generally contain endoplasmic reticulum signal sequence at their N-terminus, which directs them
to the rough endoplasmic reticulum. After completion of translation process in the RER, the
polypeptide chains get inserted into the ER membrane or into the lumen of ER.
Some proteins move to the transport vesicles, which fuse together to form cis- Golgi vesicles, the
cis-form again moves to trans-form. During this process, many proteins undergo modifications
particularly at oligosaccharide chains. From the trans-Golgi vesicles, proteins move to cell
membrane through small transportation vesicles (exocytosis).
Solution
The process of protein synthesis and secretion starts from the endoplasmic reticulum. The
polypeptide chain is formed in the ribosomes, and then transferred to the Golgi apparatus, where
the final modifications are done. The Golgi apparatus sorts the modified poly peptide molecules
and packages into new transport vesicles which reach their particular destinations. The
tranlocons transport the polypeptides with a signal sequence to the interior of the endoplasmic
reticulum. Multiple control mechanisms of the endoplasmic reticulum ensures that only properly
folded proteins to export towards the Golgi apparatus.
The plasma membrane proteins synthesized in the endoplasmic reticulum (ER). The proteins
generally contain endoplasmic reticulum signal sequence at their N-terminus, which directs them
to the rough endoplasmic reticulum. After completion of translation process in the RER, the
polypeptide chains get inserted into the ER membrane or into the lumen of ER.
Some proteins move to the transport vesicles, which fuse together to form cis- Golgi vesicles, the
cis-form again moves to trans-form. During this process, many proteins undergo modifications
particularly at oligosaccharide chains. From the trans-Golgi vesicles, proteins move to cell
membrane through small transportation vesicles (exocytosis).
