The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid. Introduction: In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

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Answer 1

Question

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

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Question #3: In the KeyGene paper, the authors state that it would be useful if pollen from an apomict would transmit apomixis-inducing genes to the female in the cross (assuming the pollen is viable). Assuming there was just one gene conferring gametophytic obligate apomixis, and that the two parents are inbreds, what would be the consequences of such a cross if: a) The apomixis was a dominant trait? Indicate the genotypes and phenotypes (apomict or non- apomict) of the parents, F1 and F2 generations. Remember to include the expected genotypic and phenotypic ratios (or percentages) in the F1 and F2 generations, and to position the female first (left side) in the parental cross. b) The apomixis was a recessive trait? Indicate the genotypes and phenotypes (apomict or non- apomict) of the parents, F1 and F2 generations. Remember to include the expected genotypic and phenotypic ratios (or percentages) in the F1 and F2 generations, and to position the female first (left side) in the…

Question #5: Assume that two genes are identified that confer gametophytic facultative apomixis in soybean. The genes show independent assortment. Recessive alleles at both loci are required for the facultative apomixis. Facultative apomixis is triggered when the temperature at pollination is above 20 degrees C. At temperatures below 20 degrees C, all reproduction is sexual, independent of genotype. A facultative apomict male, capable of producing viable pollen, was crossed with a sexually reproducing female. Assuming the parents are completely inbred, what are the predicted phenotypic ratios (apomict: non-apomict) for the F1, F2, and DH (F1-derived) generations at each of the following temperatures*: a) 15°C? b) 25°C? *for full credit, show crosses and genotypes where appropriate. Remember to position the female first (left side) in the cross. Type your answer here:

Answer 2

Question

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

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Answer 3

Question

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

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Answer 4

Question

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

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Answer 5

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

Answer 6

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

Answer 7

Chapter 18.3, Problem 8SAQ

Summary Introduction

To determine:

The change in the binding of large multisubunit protein when it binds to a small molecule no larger than one amino acid.

Introduction:

In genetic diversity the gene may be regulated in two directions one is negative regulation and other is positive regulation. To carry out the process of transcription and translation we need the main player such as DNA, RNA polymerase, and regulatory proteins which are together called as transcriptional activator. The function of activator protein involves the binding to DNA specific sequence. But sometimes it happens that the activator protein binds to the small protein molecules that alter its binding affinity for DNA.

Answer 8

Expert Solution & Answer

Explanation of Solution

When the large protein molecule binds with a small molecule of protein it leads to conformational change in the part of protein. The binding affinity of the protein alters due to change in the shape and this shows allosteric effect. Sometimes small molecules are needed for the binding of proteins to a particular sequence of DNA as it allows the change in the shape of activator protein. Thus the presence of small molecules regulates the transcription of gene. The combination of small molecule to a large protein brings structural change and its specificity for the original DNA binding site changes. It generates a new and different DNA binding specificity due to exposure of a new amino acid chains.

Answer 9

Expert Solution & Answer

Answer 10

Expert Solution & Answer

Answer 11

Conclusion

The binding of small molecule to a larger and multisubunit protein results in the structural change of protein. This results in the alteration of the amino acid change and thus the specificity for DNA binding site changes. Sometimes small molecule play significant role for binding of the protein molecule to a specific DNA sequence.

Answer 12

Ch. 18.1 - Prob. 1SAQ Ch. 18.1 - Prob. 2SAQ Ch. 18.1 - Prob. 3SAQ Ch. 18.1 - Prob. 4SAQ Ch. 18.1 - Prob. 5SAQ Ch. 18.2 - Prob. 6SAQ Ch. 18.2 - Prob. 7SAQ Ch. 18.3 - Prob. 8SAQ Ch. 18.3 - Prob. 9SAQ Ch. 18.3 - Prob. 10SAQ

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