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…
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A: sickle cell anemia is a genetic disorder caused by alternation in genetic sequence .
Q: ength of the double helix
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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…
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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…
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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…
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Solved in 2 steps
- Contribution of the features of the alpha-helix to the stability of the protein.Type of interaction that determine the conformation of polypeptide chainwhy all amino acids except glycine have L and D forms and specify the type of isomerization exhibited by by these monomer units of protein and why this matters.
- Reposting - What would the tertiary structure of the dipeptide Asp-Ser be if it was made into a polypeptide chain? (Would it form a beta pleated sheet, an alpha helix, etc) Why would it do this? What properties of this polypeptide causes this? This sub part still needs to be solved - What would the tertiary structure of Pro-ala and Glycl-L-alanine be?structure of cholesterol, define the three regions of the molecule, know that this molecule regulates membrane fluidity, and distinguish between esterified and unesterifiedcholesterolcip sequence rule in ephedrine