Trypsin cleaves polypeptide chains at the carboxyl side of a lysine or arginine residue. Chymotrypsin cleaves polypeptide chains on the carboxyl side of an aromatic amino acid residue or nonpolar, bulky side chain. Which is more specific?

Q: Classify each peptide chain as part of a parallel β sheet, part of an antiparallel β sheet, either…

A: Beta-sheets are one of the most common secondary structures seen within proteins. Several…

Q: A lysine is on the surface of a protein, near an aspartate. How does the aspartate alter the pKa of…

A: The pKa of an amino acid's side chain determines whether it is protonated (+) or deprotonated (-)…

Q: Glycosylation is a major type of protein post-translational modification. Identify the amino acid…

A: Cavalent or generally enzymatic reactions takr place after or during translation are termed as post…

Q: What is the difference between a deoxynucleotide triphosphate (dNTP) and a dideoxynucleotide…

A: dNTPs are also called deoxyribonucleotide triphosphate. Each dNTPs are made up of a phosphate group,…

Q: How do you think incorporating b-homoserine into a peptide would affect the structure and/or…

A: Homoserine, is the product of a cyanogen bromide cleavage of a peptide by degradation of methionine.…

Q: A nonapeptide was treated with dithiothreitol to reduce any disulfide bridges, then partially…

A: Amino acids are the basic unit of the peptide and proteins. They are joined via the peptide bonds to…

Q: So which form of the arginine side chain is the ionized form? And when the side chain is ionized the…

A: Arginine is an amino acid with a side chain that contains a guanidine group. In its conjugate acid…

Q: Digestion of a peptide with trypsin generates two smaller peptide products: methionine-glycine and…

A: pepsin is a serine protease that cleaves the bond present in the C-terminal of amino acids Lysine…

Q: Describe the chemical differences between a ribonucleoside triphosphate and a deoxyribonucleoside…

A: Ribonucleotide triphosphate (RNTPs) and Deoxyribonucleotide monophosphate they are used in…

Q: Shown below is an internal fragment of a polypeptide. If this polypeptide were growing, onto which…

A: Biomolecules are the biological molecules that are present inside the living organisms. These…

Q: Which form of flavin adenine dinucleotide is the "reduced" form, FAD or FADH2? Explain

A: Flavin Adenine Dinucleotide: It is a redox active coenzyme associated with various proteins, which…

Q: Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S1…

A: Serine proteases are proteolytic enzymes that cleave peptide bonds. They are hydrolases that use a…

Q: Shown to the right is a cartoon image of ETC Complex I from Y. lipolytica. A group of authors…

A:

Q: Draw a peptide bond between Phenylalanine (c-terminus) and Isoleucine (n-terminus).

A: Amino acids are organic compounds with two functional group namely carboxyl and amino. There are 20…

Q: Consider a mutation that results in a substitution of Cysteine (CYS) ) for Tyrosine (TYR) at…

A: Cysteine is a polar amino acid.  Cysteine is a triprotic acid with three ionizable functional…

Q: Why is selenocysteine called the 21st amino acid when there are many more amino acids found than the…

A: Introduction: The 21st proteinogenic amino acid is selenocysteine. It is an essential amino acid.…

Q: Consider a short peptide that forms an alpha-helix within a larger protein structure. Suppose that…

A: Amino acids are the simplest units to form peptides and proteins. The amino acid sequences represent…

Q: What do you name the binding between two amino acids?

A: An organic molecule comprised of a carboxyl and an amino group is known as amino acids. When amino…

Q: A heptapeptide that puncture the bacterial cell wall has just been recently isolated from the venom…

A: The given flowchart describes the various chemicals that the heptapeptide has been treated with and…

Q: Shown below is an internal fragment of a polypeptide. If this polypeptide were growing, onto which…

A: The incorporation of an amino acid into a protein follow specific trend with respect to the ends of…

Q: Trypsin cleaves proteins on the carboxyl side of lysine. Trypsin inhibitor has a lysine residue, and…

A: Introduction: An enzyme is the catalysts that increase the rate of reaction without undergoing any…

Q: How do you think incorporating a-methylserine into a peptide would affect the structure and/or…

A: proteins are made up of amino acids . amino acid polarity and peptide struture depends upon the side…

Q: In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-…

A: A helical wheel representation is a type of plot or visual representation used to illustrate the…

Q: To visualize the spatial arrangement of amino acid residues in an a-helix, it is helpful to imagine…

A: Alpha helix is a secondary structure of protein. The alpha-helix can be right-handed or left-handed.…

Q: Throughout the polypeptide chain, must the amino acid residues at the active site be next to one…

A: A polypeptide chain is a lengthy sequence of amino acids that contains amino acid residues that…

Q: Consider an amino acid sequence:…

A: Since you have posted a question with multiple sub-parts, we will solve first three sub-parts for…

Q: What kind of repeating polynucleotide would yield a single polypeptide with a tetrapeptide repeating…

A: Polynucleotide is a sequence of nucleotides. Nucleotides consist of a sugar molecule, a phosphate…

Q: What is the number of possible linear oligopeptides with 4 polar uncharged amino acid residues?

A: The objective of this question is to determine the number of possible linear oligopeptides that can…

Q: Describe the chemical differences between a ribonucleotide triphosphate and a deoxyribonucleotide…

A: Nucleotide are group which form DNA or RNA .It generally consists of :-  A ) Nitrogenous base  B )…

Q: The enzyme creatine kinase catalyzes the ATP-dependent phosphorylation of creatine. Propose a…

A: Introduction:  Creatinine is the waste product formed in muscle from a high-energy storage compound…

Q: Sickling occurs in deoxyhemoglobin S but not in oxyhemoglobin S. Oxyhemoglobin has a small,…

A: Sickling is the process where the haemoglobin protein inside the RBC cell clumps together this…

Q: Given the peptide Val-Ser-Gln-Lys The lateral chain of one of these amino acids can be modified by…

A: During N-terminal acetylation, an acetyl group (CH3-C=O-) is added to the N-terminal amino group…

Q: I'm conducting an experiment concerned with the binding affinity of tretinoin (all trans retinoic…

A: Fluorescence resonance energy transfer (FRET) is a mechanism of energy transfer between two light…

Q: The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond…

A: The alpha helix orientation of the polypeptide is possible because of the groups of amino acids in…

Q: A peptide with endorphin-like property was produced and obtained from the blood. This was sequence…

A: Protein degradation is the process of protein digestion using proteases. Proteases specifically…

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.