8 ) Solution :
In some conditions the proteins are able to bind to a small molecule which are known as ligand by the weak interactions such as ionic bonds hydrogen bonds, hydrophobic effects and Vanderwaals interactions
Example of a ligand is oxygen , it is a ligand which binds to both haemoglobin and myoglobin.
9 ) Solution :
The 4 ways that protein function is regulated are as follows
1 . Due to non covalent binding of small molecules i.e., amino acids or nucleotides are involved in the regulation of protein function by causing a change in the conformatiion and finally the activity of protein .
2 . Phosphorylation is also regulates the funtion of protein i.e., addition of phosphate groups to specific amino acids on the protein . This process is also reversible and serves as a handy switch on-off
3 . Interactions among the polypeptides making up the protein, or between the protein and other proteins in the cell are also involved in the regulation of protein function
4 . Protein posttranslational modifications regulates the protein function by obtaining a small changes to their basic chemical structure .These posttranslational modifications can profoundly alter a protein’s activity, localization, stability, and/or binding partners, and therefore constitute the “front line” of many signaling systems within the cell.
8. How do proteins interact with ligands? (What holds them together?) 9. What are the FOUR...
Based on the figure, how do you think each of the four proteins function in the cell? mature mRNA A | 1 | 2 | 3 4 | 6 | 7 | 8 | 9 | 10 | mature mRNAB | 1 | 2 | 3 | 4 NEN 6 7 8 9 10 mature minacC1 | 2 | 3 | 4 | 6 | 7 | 8 | 10 | mature mRNA D 1 2 3 4 NN 6178...
5. What do proteins do for your body? 6. What holds the sides of the DNA ladder together? 7. What are the sides of the DNA ladder made of? 8. What three parts make up a single nucleotide?
3. The structure and properties of amino acids and the peptide bonds that link them together determine the structure and properties of proteins. Explain how amino acids and peptide properties dictate protein structure and, therefore, their function.
What are two major types of protein secondary structure, and what kind of interaction holds them together , and between what part of the protein do they occur?
1. How do prokaryotes conserve energy? 2. How do DNA-binding proteins in prokaryotes regulate genes? 3. What is an operon? 4. What is in the lac operon in E. coli? 5. What is the function of the genes in the lac operon of E. coli? 6. What turns the lac operon off? 7. How does a repressor protein turn off the lac operon? 8. How does lactose turn on the lac operon?
Proteins are long chained polypeptides that are biologically active. Describe what comprises proteins and how proteins may be formed. What are the different classes of proteins? What are the various layers of structure to a protein? Describe what each layer entails or describes. What are the various ways to disrupt a protein? Are there mechanisms which will “kill” a protein that are not outlined in the text?
please answer 1 a-f 1. Explain how G proteins are regulated. Include in your answer a description of the functions of GTP binding, GTP hydrolysis, and GDP exchange for GTP in terms of effector activation, as well as the functions of regulatory proteins GEFs, GAPs, and GDls. (12 points total, 2 points each) A. Function of GTP and GDP binding on G protein activity B. Impact of GTP/GDP on G protein binding to an effector C. Role of G protein's...
In-Class Activity #12, Protein Tratlicking Worksheet 1. You are interested in four different proteins in a yeast cell: • protein 1 is a cytosolic protein protein 2 is a secreted protein • protein 3 is a nuclear protein protein 4 is a cell surface membrane protein with N-terminal end in extra-cellular space. a. You plan to study how the proteins are localized to their specific destination by creating the following mutations in the genes encoding proteins 1-4. Indicate how the...
14. What is Hydrophobicity Scale? Classify the amino acids according to this scale. How do surface and core a protein differ? 15. Describe the three common ways to stabilize protein structures? 16. What are some substances that will denature proteins? How do they cause denaturation? How can renaturation of a protein be brought about? 17. What is the function of molecular chaperones?
1. Describe a typical protein-protein interface, and what is required to allow for protein interactions. 2. Are NAD- and ATP-binding domains generally conserved or unique? Why? 3. Why do proteins have cofactors (what role do they serve)? 4. Describe the two ways proteins can interact with DNA, and the differences between both. Which is similar to the RNA recognition motif? 5. How do proteins differentiate between ssRNA, dsRNA, DNA-RNA hybrids, and dsDNA?