Which of the following characterize -helix regions of proteins? (A) They all have the same primary structure. (B) They are formed principally by hydrogen bonds between a carbonyl oxygen atom in one peptide bond and the amide hydrogen from a different peptide bond. (C) They are formed principally by hydrogen bonds between a carbonyl atom in one peptide bond and the hydrogen atoms on the side chain of another amino acid. (D) They are formed by hydrogen bonding between two adjacent amino acids in the primary sequence. (E) They require a high content of proline and glycine

Q: Which of the following might cause the denaturation of a protein? Select all that apply. A.)Highly…

A: Biological macromolecules are the molecules that are needed in a sufficient quantity for the…

Q: In most cases the peptide bond is in the trans conformation. What statement below best explains this…

A: In proteins the adjacent amino acids are held together via peptide bonds . A peptide bond is an…

Q: Draw the following Lipids in: A) Condensed (detailed) Structure, B) its Block Diagram. C)…

A: Lipids are a chemically diverse group of biomolecules that have two things in common: low…

Q: Which is an appropriate statement of involvement of the hydrophobic effect in protein folding? A)…

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

Q: a) Can a carbon with a double bond have a D or L designation? Explain. b) name and describe the…

A: There are different kinds of biomolecules are present in the body. Carbohydrates, protein, lipids,…

Q: Which of the following (could be more than one) would not be a rational explanation for why the…

A: A protein's three-dimensional structure, also known as its "3D structure" or "tertiary structure,"…

Q: Which dastardly proteins help polypeptides fold into an incorrect and non-functional state?

A: Protein synthesized by ribosomes associated with the membrane of the Rough endoplasmic reticulum…

Q: The nucleic acid bases: A)absorb ultraviolet (260 nm) light. B)have all of these described…

A: Introduction: Nucleic acids are one of the major macromolecules present mainly in the nucleus of the…

Q: The amino acid that lacks a backbone NH for bond formation to backbone CO group (due to the presence…

A: Amino acids commonly called alpha-amino acids because of a primary amino group(-NH2 ) and a…

Q: 1. Proteins, structurally and functionally, are the most diverse molecules in life. The shape of a…

A: Proteins are the polypeptide chain of amino acids are arranged in a specific order. The proteins are…

Q: The substitution of one amino acid for another in a polypeptide chain can affect the __________ of…

A: Proteins are needed for growth and maintenance and they also provide structural support to the…

Q: For each of the following amino acids: 1) describe what the important functional group of the amino…

A: Proteins are made up of amino acids. Each amino acid has a distinct side chain, also referred to as…

Q: Which of the following amino acids has a hydrophobic R-group and would tend to be found on the…

A: Introduction:  Amino acids are molecules that contain an amine group, carboxylic acid group, and a…

Q: (a). Name the TWO functional groups that are characteristic of all amino acids. (2) (b). Assume that…

A: The amino acids are monomers of proteins. Individual  amino acids are zwitterionic in nature which…

Q: In the peptide Ala – Gly – Val – Phe – Tyr, a carboxylate (-COO-) group would bound in which amino…

A: The four types of biological macromolecules are proteins, nucleic acids, lipids and…

Q: 1. What is one structural difference between: Glucose and starch   (Choose one answer for the above…

A: 1.Hydrocarbons: glucose & starch: organic compounds generally made of carbon and hydrogen as…

Q: Consider the sequences (i-iv) that represent sections of a protein. i) -AEEAAAAMAAAAMAAY ii)…

A: Secondary structure is the formation of regular patterns through interaction between nearby…

Q: 10) Denaturation of a protein

A: Proteins are complex structures that play a variety of important roles in the body. These are…

Q: The sidechain of the amino acid serine is -CH2-OH. Serine is classified as this type of amino acid…

A: Serine is a non-essential amino acid in humans. It is present and functionally important in many…

Q: Proteins are sometimes classified as being globular proteins or fibrous proteins based on their…

A: The proteins that have long and narrow shape with structural role can be defined as fibrous proteins…

Q: 7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic…

A: Proteins - Proteins are the macronutrients which are used for the building up of the muscles in the…

Q: How many amino acids and peptide bonds does a tetrapeptide have?

A: Ans- A) four amino acids and three peptide bonds Tetrapeptide is a peptide also known as…

Q: Explain 3 benefits of proteins forming higher oligomeric states.

A: Protein is a macronutrient needed to build muscle mass. It is found in animal products, even though…

Q: What are the four different levels of a protein structure?

A: Proteins are the building blocks of life. They are the most common molecules found in all cells.…

Q: Which of the following statements about alpha-helix and beta-sheet structure are true? More than one…

A: A protein's function depends on its structure. There are four levels of protein structure: primary,…

Q: (1) (2) (3) Which of the following residues would be most likely to make contact with the aqueous…

A: Proteins are intricate macromolecules made up of a large number of amino acids that are connected by…

Q: Which of the following levels of protein structure may be affected by hydrogen bonding? (a) primary…

A: Protein is a biomolecule that comprises one or more long chains of amino acids that belong to the…

Q: Give the force of interaction involved in the protein folding of the protein structure A and C: COO…

A: Protein folding is the process in which the primary structure is transformed into the functional…

Q: Which best describes the contribution of primary (1’) structure of polypeptides to the native…

A: Protein structure:  Primary  Secondary Tertiary  Quaternary

Q: What kind of bond would you expect between the side chains of the following amino acids?(a) Cysteine…

A: Amino acids are molecules which when combined together forms a macromolecule known as protein. It…

Q: Which statement about the structure of proteins is correct? a) The a-helix and ß-sheet are two…

A: Proteins are complex biomolecules that are essential to the functioning of living organisms. They…

Q: Having peptides arranged in a beta sheet would be an example of a secondary structure A) True B)…

A: Peptides and polypeptides are linear and unbranched polymers composed of amino acids linked together…

Q: A) Refer to the figure below, Identify and explain the two types of reactions, and describe what are…

A: Metabolic reactions are the chemical reactions that take place in our body for the conversion of…

Q: This amino acid is: (Note that the non-ionized form is shown; remember that backbone groups are…

A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…

Q: Draw the following Lipids in: A) Condensed (detailed) Structure, B) its Block Diagram. C)…

A: Phospholipids are compound lipids composed of fatty acid, alcohol, nitrogen containing molecules,…

Q: Φ and ψ in the Ramachandran plot (below) are: a) Rotational angles around the bond between the…

A:

Q: What type of bonds/forces stabilize protein secondary structure?

A: Solution -  Protein structure -  The structure of a macromolecule determines its function. The study…

Q: (a) A protein is found to be a tetramer of identical subunits. Name two symmetries possible for such…

A: Tetramer : It is an oligomer formed from four monomers or subunits. The associated property is…

Q: Consider a protein with a beta conformation sequence EAGQVHRGP a) Which residue(s) can be…

A: Beta conformation in protein: Beta sheet, beta-turn etc are beta conformation in protein. Beta sheet…

Q: Peptide bonds cannot rotate. This is because: a) the amino acid side chains are too bulky to allow…

A: The peptide bond contains an amide type function group. It is formed by the two amino acid, that is,…

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.