S-S S-S- S-S Case #1: Case #1: Disulflde forms Disulfide forms In near temini mlddle of proteln

Q: Which of the following would be considered a severe mutation? A) Leucine (Leu) > Lysine (Lys) B)…

A: Amino acids are classified based on their properties like whether they are polar or nonpolar,…

Q: As part of a project investigating potential new drug targets in the fight against malaria, you are…

A: Introduction:-  Truncation of protein:- is meant by the proteolysis or structural gene manipulation…

Q: what would the net charge on the tetra peptide of sequence ala-lys-glu-ser at ph 7.2 what would it…

A: Amino acids are the building blocks of proteins or peptides formed of chiral carbon having four…

Q: the peptide (written N-terminal to C-terminal) represented by Ala-Ser-Ala-Tyr the same as the…

A: Ans. Yes, the polypeptide chain of amino acid will be Similarly in structure and function whether it…

Q: How is the peptide shown named (give each 3-letter name for the amino acids present)? Whichamino…

A: The peptide is made up of amino acid. The sequence of amino acid in this peptide is N - Val-Phe-Trp-…

Q: The antiparallel b-sheet motif, first discovered by Linus Pauling, is found in which of the…

A: When two or more polypeptide chains are held together by intermolecular H-bonds the structure is…

Q: A particular protein has the amino acid sequenceN . . . Ala-Pro-His-Trp-Arg-Lys-Gly-Val-Thr . . .…

A: The mutation occurs when there is an error in the sequence of the DNA. It could be because of the…

Q: n as1 mutant, assign secondary structure and tell how many alpha helices and beta-pleated sheets…

A: Primary Structure: It is defined as a linear sequence of amino acids joined to each other through a…

Q: What is single-cell protein? Explain the reasons for the removal or reduction of nucleic acid in…

A: Protein is a substance formed of amino acids joined by peptide bonds. Nucleic acid - are compounds…

Q: . Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold).…

A: In disulfide linkage, the two cysteine amino acids are joined by a disulfide bond.

Q: What are the possible codons that a tRNA molecule could interact with if it is carrying each of the…

A: A codon is a triplet nucleotide of DNA or RNA corresponding during protein synthesis to a particular…

Q: A comparison of the aligned amino acid sequences of two proteins each consisting of 150 amino acids…

A: Introduction Stating evolutionary relationships between two proteins or their domain still leaves a…

Q: Which of the sequences below do you think would most likely be found in an intrinsically disordered…

A: Intrinsically disordered proteins (IDPs) are those that do not have a proper three-dimensional…

Q: A scientist wants to use a technique that allows to shuffle protein domains. Protein A and Protein B…

A: Ans: Protein domain: The protein carries separate region in the polypeptide protein which shows…

Q: A common strategy for identifying distantly relatedhomologous proteins is to search the database…

A: Introduction: Bioinformatics is an interdisciplinary field of science that combines biology,…

Q: You are trying to isolate a protein you don't know much about, so you decide to use a gel column…

A: Introduction :-  Chromatography is a biophysical technique which is used to separate or isolate the…

Q: В C as1 wild type as1 mutant as1 superimposed A

A: Alpha-helices and beta-sheets are called the secondary structures of the protein. Secondary…

Q: What are the properties of the wild type amino acid, Tyrosine at position 368?  Hint: the amino…

A: Tyrosine is an aromatic protein.

Q: A normal hemoglobin protein has a glutamic acid at position 6; in sickle-cell hemoglobin, this…

A: In the normal hemoglobin molecule protein, has a glutamic acid (an amino acid) at the sixth position…

Q: A protein with which of the following sequences may be more prone to undergo farnesylation? (a)…

A: Prenylation (or lipidation) is a process of "post-translational modification" (PTMs) of proteins by…

Q: Imagine a globular protein with a histidine that is involved in a salt bridge to an aspartic acid,…

A: Globular proteins are a group of protein sub-types. They form colloids  and are somewhat soluble in…

Q: that the

A: Polypeptides, or proteins, are chemical compounds composed up of amino acids. They're big,…

Q: A solution of a peptide of unknown sequence was divided into two samples. One sample was treated…

A: Only twenty of the available amino acids are often present in proteins among all the possible amino…

Q: If a new isolated protein called STICKY and this STICKY protein contains a bHLH domain. Now, how we…

A: Protein motifs are the distinct conserved small polypeptide sequence in proteins. These super…

Q: You have discovered a novel protein that has a pI = 5.5. To study the functional properties of this…

A: Isoelectric Point (pI) is a condition at a particular pH where the amino acid is present in the…

Q: You have discovered a novel protein that has a pI = 5.5. To study the functional properties of this…

A: The functional properties of the new protein, has two amino acid changes—namely, a surface Phe…

Q: The limit for G-200 beads is 5000-600,000. When you pass two proteins- Protein A (75, 000), Protein…

A: Proteins are amazing molecules that make everything simple inside the cell. Protein molecules are…

Q: (a) How many activation cycles are needed for a protein with 150 amino acids? (b) How many…

A: The process of translation or protein synthesis occurs in the cytoplasm of a cell in both…

Q: Why is the euchromatic region or light bands in G banding rich in Guanine and cytosine? And why is…

A: euchromatic region or light bands in G banding rich in G C while dark region rich in AT.

Q: 1. For each of the sequences given below, list what type of secondary structural element, if any is…

A: Proteins are found in four structures namely:  Primary which is a linear sequence of amino acids.…

Q: A recent genome sequencing project for the bacterium Burkholderia mallei has identified a new…

A: The new protein identified here has a partial sequence given as TVEVNAPGDVQKALSELQQINDGRLDIRI…

Q: Based on the N-terminal amino acid sequence, what is the approximate half-life of the protein after…

A: Introduction- N-terminal methionine cleavage plays an important role in protein synthesis in…

Q: The so-called kelch motif consists of a four-stranded β sheet, which forms what is known as a β…

A: Introduction Proteins are huge biomolecules and macromolecules that are made up of one or more long…

Q: Describe the planar sections of the primary sequence, their influence on the shape of the protein…

A: Amino acids are the building blocks of proteins. These are compounds containing Carbon, Hydrogen,…

Q: What is the function of the molecular chaperone? What would happen to the protein if molecular…

A: According to the question we have to give the function of the molecular chaperon. In addition to…

Q: How can widely separated parts of a protein interact with the spike protein

A: Spike proteins are glycoproteins that are present on the surfaces of the enveloped viruses of many…

Q: How would the the triple mutations K557R and D591V and K617A alter the overall protein?

A: Here,  1.) K means lysine(positively charged amino acid) 2.) R means Arginine(positively charged…

Q: and Arg29 is important in determining the structure of the protein. a) What type of amino acid is…

A: This is a question about protein fold and the importance of amino acids in folding.

Q: Assume you were given a mixture consisting of one molecule each of all possible sequences of a…

A: Proteins are long chains of single amino acids. The human body uses 20 different amino acids in…

Q: Low-resolution X-ray diffraction analysis of a protein composed of long stretches of the sequence…

A: Fibroins are insoluble proteins that are present in silk produced by insects, such as the larvae of…

Q: You have discovered a novel protein that has a pl = 5.5. To study the functional properties of this…

A: In this mutation process, hydrophobic phenylalanine is replaced by the Histidine residue. Histidine…

Q: Can you describe the ensemble allostery model and explain how it is used to explain allostery in…

A: In allosteric regulation binding of a ligand to one of the subunit enhances or decreases the binding…

Q: You have a mixture of positive, negative and neutral proteins. In order to obtain a pure positively…

A: Proteins are composed of amino acids, which are bound together by peptide linkage. Amino acids…

Q: Describe why this position in your protein is important and outline the effects the mutation will…

A: Any change in DNA is referred to as a mutation. Any heritable and genetic modification in the genome…

Q: A mutant is found that has the following protein sequence: Met Gly Thr Leu Arg Gly. What is the…

A: Mutation is defined as the alteration in gene that result in alteration in the function of the…

Q: Do you think it is possible that interchain disulfide bonds is present in the protein? Explain. b.…

A: Disulfide bond is the post-translational modification occurs in Endoplasmic reticulum. Disulfide…

Q: PLEASE DONT COPY IN GOOGLE OR HERE ON BARTLEBY. Salt bridges are more commonly formed compared to…

A: Introduction: The fundamental driving force behind the folding of a protein is energy. A folded…

Q: What is the resulting polypeptide: _______________________________________________________? What…

A: Biomolecules are organic molecules present in living organisms. They include carbohydrates,…

Osmosis

In simple words, osmosis is the slow, gradual movement of a liquid through a membrane. But there are nuances to this process. For instance, there has to be an imbalance in the distribution of solute in the liquid on either side of the membrane, which has to be semipermeable. The liquid in the region with a lower solute concentration moves to the region with a higher concentration, thereby displacing the solution in the process. The objective is to equalize the concentration of molecules on both sides of the membrane; the displacement of liquid can be viewed as a byproduct of this equalization. Since there is no energy required to carry osmosis, it is considered a passive process.