Peptide bond properties. How these properties determine the three-dimensional structure of the protein.
Q: V-B. Which of the following peptides would be more soluble at the indicated pH? 1. (Gly)20 or…
A: The twenty amino acids are classified into majorly the following classes: Polar Nonpolar Positive…
Q: Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral…
A: Introduction: Amino acids are a group of organic compounds containing two functional groups- amino…
Q: The defining characteristics of amino acids and how the 20 amino acids involved in protein structure…
A: Each of the 20 most common amino acids has its specific chemical characteristics and its unique role…
Q: how cohesin acts as the glue
A: Cohesin is a complex of multiple protein units that is responsible for holding together the sister…
Q: Red blood cells are normally circular in shape. Sickle cell anemia is a disorder that affects the…
A: sickle cell anemia is a genetic disorder caused by alternation in genetic sequence .
Q: ength of the double helix
A: Gene: The gene is a sequence of nucleotides in DNA or RNA which encodes the synthesis of a gene…
Q: Structure of globin mRNA
A: The cell consists of the genetic material, which can be either DNA or RNA. DNA is the…
Q: how the structure of arachidonic is suited for the synthesis of PGG2.
A: Prostaglandins are C20 fatty acids that have been changed and produced in animal tissues. They have…
Q: Thinking about the complexity of biochemical systems as they relate to the human body and the…
A: DNA which is deoxyribonucleic acid plays as the hereditary genetic material in humans and almost all…
Q: The simplest water-friendly, amino acid, which has only a single carbon in it's R chain, just like…
A: Introduction: α-amino acids are the building blocks of proteins. These organic molecules contain two…
Q: Połymer formation from a pool of available monomers with a range of chemical functionalities…
A: Introduction:- The quetion is about the biomolecules that are polymers that made up of small units…
Q: Replacements such as Lysine -- Arginine and Leucine -- Isoleucine usually have very little effect on…
A: Characteristics of amino acids: Amino acids are the nitrogenous monomeric units of biomolecules…
Q: Give a brief description of what the term ‘native protein’ state refers to. Your answer should make…
A: Introduction: Proteins are biological polymers made up of amino acids connected covalently by…
Q: Color Reactions of Intact Protein: 1ml of water and 0.5 g of casein 1ml of water and 0.5 g of bean…
A: All proteins do not contain the same amino acids hence they do not respond to all colour reactions…
Q: Suggest an explanation for the observation that when proteins are chemically modified so that…
A: A polypeptide chain is made on cellular structures, called the ribosomes. This is done by a complex…
Q: Definition of the concept of "amino acid". The main parts of the amino acid molecules. Alpha, beta,…
A: Amino acids are building blocks of proteins, which polymerize to form different kinds of proteins.…
Q: Hydropathy plot analysis of your protein of interest reveals a single, prominent hydrophobic peak.…
A: The hydropathy plot, in the case of proteins, gives the idea about the hydrophilic and hydrophobic…
Q: biochemical aspects of phenylketonuria disease
A:
Q: A common calcium-binding motif called the __________ contains twoshort helices connected by a loop
A: Calcium-binding proteins are responsible for binding to calcium. Various types of calcium-binding…
Q: Protein Description A 35 kDa monomer Disulfide-linked homodimer comprised of 19 kDa monomers…
A: Protein is made by amino acids and in living organisms, 22 types of amino acids exist and each has a…
Q: Although the Shine-Dalgarno sequences vary considerably in different genes, they include examples…
A: The Shine–Dalgarno sequence is a binding site on the ribosomes of archaeal and bacterial mRNA…
Q: Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following: a.…
A: Note: Since you have asked for multiple subparts, we will solve the first three for you. If you want…
Q: The ability of molecules to exist in two non- superimposable (mirror-image ) way called chiral, in…
A: Enantiomers are the chiral molecules that consist of mirror images or non-superimpossible molecules.…
Q: The manner in which nucleic acids join together forms a _________________-_________________…
A: Nucleic acids are made up of nucleotides. A nucleotide is made up of a nitrogenous base, a sugar…
Q: A secondary structure of proteins in which the peptide has regular coils and every N-H group…
A: Local folded structures that arise within a polypeptide as a result of interactions between backbone…
Q: Shape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled…
A: Secondary structure of protein: Formed due to twisting of polypeptide chain.The folding is due to…
Q: Suggest a reason why amino acids are usually more soluble at pH extremes than they are at neutral…
A: There are about twenty essential and nonessential amino acids are often present in proteins. Amino…
Q: the major components of complex biomolecules. For each of the two important biomolecules below…
A: GTP is an energy-rich molecule, just like ATP. Usually when it is hydrolyzed, the free energy of…
Q: Protein solubility
A: here they are talking about protein solubility. Protein solubility is a thermodynamic property…
Q: Pro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.
A: Proteins are one of the most important macromolecules. They form the building blocks of all…
Q: Briefly explain why the size and weight of a protein are not directly proportional to the number of…
A: Proteins are biopolymers made of amino acid units. Amino acids are comprised of carbon, hydrogen, a…
Q: The chemical structures of the two opposing ends in any polypeptic because: O a. the structures of…
A: A polypeptide is a string of covalently bonded amino acids that has not been folded into a…
Q: How multiple domains in a single protein increases the versatility of each molecule ?
A: A protein domain is a region in a protein molecule or polypeptide chain of protein which is…
Q: A biochemistry student characterizes the process of cooking meat as an exercise in denaturing…
A: Meat consist of various type of protein such as actin, myosin, etc., The myosin and actin play an…
Q: Compare and contrast structural features of collagen and α-keratin (OK to do this as a list or table…
A: Proteins are polypeptides. They are linear chains of amino acids linked by peptide bonds. Each…
Q: Each sequence of three bases called a
A: Both DNA and RNA are made of nucleotide bases.
Q: - TRUE about the peptide bond:
A: With the loss of a water molecule, a covalent link is formed between the - carboxyl group of one…
Q: Classification of amino acids by radicals, on what it is based. Name and draw radicals of each type…
A: The amino acids are compounds containing carbon, hydrogen, oxygen, and nitrogen. They act as the…
Q: Formation of peptide bonds, di- and tripeptides and their nomenclature. Examples of synthetic…
A: Proteins are the polymers of amino acids. Amino acids are joined together by peptide bond.
Q: Peptide bond is /has ……………. This structural feature prevents protein to sample all possible…
A: In a protein or a polypeptide chain, two amino acid molecules are joined together by a peptide bond.…
Q: How an alpha helix and a beta pleated sheet differ from one another
A: Every function in the living beings depends on proteins. There are many different types of proteins…
Q: Reversible denaturation of the proteins during salting out and precipitation.
A: As different proteins have different compositions of amino acids, different protein molecules…
Q: Why RNA has uracil nitrogenous base instead of thyamine ? Suggest a reason why it is more desirable…
A: RNA is very similar to DNA, but differs in a few important structural details: RNA is single…
Q: the relationship between mutation of RECQ5 and human disease, in particular exploring the effects on…
A: RECQ5:- it is a type of helicases. It is an ATP dependent helicase that can binds with single…
Q: A secondary structure of proteins in which the peptide has regular coils and every N-H group…
A: Depending on the primary structure (amino acid sequence) of the peptide, it either forms alpha-helix…
Q: Suggest why ribosomes exist as two subunits in all forms of life rather than as a single, larger…
A: Ribosomes have 3 binding sites, the A site, the p site and the E site. A loaded tRNA is brought into…
Q: structure of phenylalanyl tyrosyl seryl histidine
A: Amino acids are biomolecules that are composed of carbon, hydrogen, oxygen, and nitrogen molecules…
Q: Purification of a new unknown protein that you isolated from tissue and Assume that you have reached…
A: Guanidium hydrochloride is one of the powerful denaturants. At higher concentration of guanidium-HCL…
Step by step
Solved in 2 steps
- Beta folding. Parallel and antiparallel beta folding sheets (be able to draw). Beta loops. Examples of proteins formed mainly by this structure.Shape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?Alpha-helix of proteins, its characteristics. Draw a diagram of the arrangement of amino acids in the alpha helix. Examples of proteins formed mainly by this structure.
- Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?Ionization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. 1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state? 2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently. 3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?Instruction for the said activity: Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. d. Alanyl-phenylalanine- aspartate- cysteine e. Threonyl- Isoleucyl-methionyl- leucine f. Lysyl-alanine -Phenylalanyl-tyrosyl- serine
- Sedimenting spheres. What is the dependence of the sedimentation coefficient s of a spherical protein on its mass?How much more rapidly does an 80 -kDa protein sedimentthan does a 40-kDa protein?Protein folding with PDI and Peptidyl-prolyl isomerasetrue or false1. In the structural characteristics of a nucleotide, the phosphate subunit is bonded to the sugar subunit.2. In the structural characteristics of a nucleotide, the nitrogenous base subunit is bonded to the phosphate subunit.
- Enzyme: Crystal Structure of Wild-Type Human Phosphoglucomutase-1 (PGM1) the description of the mechanism of how this enzyme is regulated (e.g., depending on the enzyme, the mechanism could range from being solely dependent on gene regulation to protein structure-based mechanism).Vertebrate proteins? What is meant by the term polypeptide backbone?CENTRAL DOGMA & STRUCTURE-FUNCTION RELATIONSHIPS IN PROTEINS You are a bacteriologist studying a pathogenic protein (the "BAD" protein) that contributes to diseases caused by Staphylococcus aureus. BAD functions as an aß heterodimer, and the a subunit (25kD) and ß subunit (75KD) are held together by an electrostatic interaction between K in the a subunit and D in the B subunit. You are trying to dissociate the BAD subunits to prevent pathogenesis in the bacteria. Which mutation would you make to prevent the BAD subunits from forming a dimer? Assume neutral pH. (A) introduce AAA → AGA point mutation in the a subunit gene (B) introduce GAC → GAG point mutation in the ß subunit gene (C) introduce GAT → CGT point mutation in the ß subunit gene (D) introduce two point mutations: AAG → GTG in the a subunit gene & GAC → CTC in the B subunit gene (E) introduce two point mutations: AAA → TGC in the a subunit gene & GAT → TGT in the B subunit gene second base in codon A TGT Cys TGC Cys TTT Phe…