When the two domains are located in two different proteins to preserve the same functionality their close proximity and interaction have to be preserved as well?
Table of Contents
- 1 When the two domains are located in two different proteins to preserve the same functionality their close proximity and interaction have to be preserved as well?
- 2 Do different protein domains have different functions?
- 3 What is the main difference between protein domains and protein subunits?
- 4 Do all the proteins with similar functions have same motif?
- 5 What is a hydrophobic region?
- 6 Which part of protein is hydrophobic?
When the two domains are located in two different proteins to preserve the same functionality their close proximity and interaction have to be preserved as well?
Explanation: When the two domains are located in two different proteins, to preserve the same functionality, their close proximity and interaction have to be preserved as well. Therefore, by studying gene/protein fusion events, protein–protein interactions can be predicted.
Do different protein domains have different functions?
Domains are distinct functional and/or structural units in a protein. Usually they are responsible for a particular function or interaction, contributing to the overall role of a protein. Domains may exist in a variety of biological contexts, where similar domains can be found in proteins with different functions.
Which of the following is incorrect regarding 2D page?
2. Which of the following is incorrect regarding 2D-Page? Explanation: It is a high-resolution technique that separates proteins by charge and mass. It works to separate proteins by isoelectric points (pI) and then in an orthogonal dimension under a denaturing condition to separate proteins by molecular weights (MW).
Which of the following is untrue about Sage Mcq?
Which of the following is untrue about SAGE? Explanation: It is generally determined on a case-by-case basis. As a rule of thumb, 10,000 clones representing approximately 500,000 tags from each sample are sequenced. The scale and cost of the sequencing required for SAGE analysis are prohibitive for most laboratories.
What is the main difference between protein domains and protein subunits?
A domain refers to a particular region of a protein that has a specific three-dimensional structure, like a sheet or a spiral. A subunit refers to a group of proteins that are part of an even larger protein (e.g., the constituent protein groups in a ribosome).
Do all the proteins with similar functions have same motif?
Now however, several have been identified of proteins that have been identified that have different functions but which have converged to a similar fold. We found that all the similarities between structures are present in small proteins and occur as motifs within the core of a larger protein.
Can the two proteins have different properties?
Recall from Chapter 2 that there are 20 types of amino acids in proteins, each with different chemical properties. Each type of protein has a unique sequence of amino acids, exactly the same from one molecule to the next. Many thousands of different proteins are known, each with its own particular amino acid sequence.
How can you get two different proteins from the same copy of a gene?
One gene can produce one protein or several proteins through mechanisms controlling transcription, mRNA processing, translation, and posttranslational events. In yeast, changes in gene transcription and the regulation of mRNA translation play critical roles in the response to oxygen availability.
What is a hydrophobic region?
Abstract. The hydrophobic part of the solvent-accessible surface of a typical monomeric globular protein consists of a single, large interconnected region formed from faces of apolar atoms and constituting approximately 60\% of the solvent-accessible surface area.
Which part of protein is hydrophobic?
Hydrophobic amino acids are those with side-chains that do not like to reside in an aqueous (i.e. water) environment. For this reason, one generally finds these amino acids buried within the hydrophobic core of the protein, or within the lipid portion of the membrane.