Answered: Having peptides arranged in a beta…

Science

Biochemistry

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

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Related questions

Q: For i) fresh milk casein, ii) raw egg protein, explain from the protein structure why it can…

A: Casein is the major protein component found in milk. It is generally a phosphoprotein which is…

Q: t hemoglobin

A: N. Answer D Hemoglobin is an example of a globular protein. Hemoglobin is a tetrameric protein…

Q: Refer to the structure of cholesterol: a) Is the molecule amphipathic? b) Use the structure to…

A: Cholesterol has played an important role in every cell in our body, especially abundant on the cell…

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: In the deoxy state, Histidine forms an ______ salt bridge with aspartate and an ______ salt bridge…

A: A salt bridge is a non-covalent interaction between hydrogen bonding and ionic bonding. A salt…

Q: ___ fatty acid chain length, as well as ___ the number of double bonds has the effect of increasing…

A: Ans- Decreasing the fatty acid chain length, as well as increasing the number of double bonds has…

Q: What is an example of a quaternary protein structure? a) polypeptide chain b) a complete protein Oc)…

A: Proteins are large biomolecules that play very important biochemical as well as physiological roles…

Q: Chemistry A homotetramer (lacking intermolecular covalent interactions) has a native molecular size…

A: Protein structures are organized into four structural levels of organization: primary, secondary,…

Q: Using condensed structures, supply an outline of the mechanism for the formation of Gly-Gly in the…

A: During peptide bond formation the carboxylic acids and primary or secondary - amines do not undergo…

Q: Which type of interaction commonly persists even after urea is added to proteins for denaturation?…

A: Protein is a macromolecule made of amino acids. Several amino acids join together to form a…

Q: 1) A ligand-binding protein showing negative homotropic cooperativity? a) should give an nH value…

A: Cooperativity or cooperative binding occurs when binding of one molecule influences the affinity of…

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: 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: Intramolecular ______ are responsible for formation of the most common three-dimensional shape in…

A: Proteins are unbranched polymers constructed from 22 standard a-amino acids. They have four levels…

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: β-mercaptoethanol ____, and urea _____ disrupt the interactions involved in formation of α-helices.…

A: DNA stands for deoxyribonucleic acid. It is the genetic material of the organisms that transfer from…

Q: Which method for determining protein structure involves cleaving proteins into smaller polypeptides…

A: Protein structure refers to the three-dimensional arrangement of amino acid residues in a protein…

Q: Indicate which of the following properties depend only on the chemical nature of its repeating…

A: DNA is the hereditary material found in all organisms. The main function of DNA is to store genetic…

Q: RNA differs from DNA in that: a) The ribose in RNA nucleotides contains fewer oxygen atoms than does…

A: DNA = Deoxyribonucleic acid is a polymer. Which is composed of two polynucleotide chain. That chain…

Q: The dominant motif found in hemoglobin and myoglobin is: a) twisted beta sheet b) beta barrel c)…

A: 1)The dominant motif found in hemoglobin and myoglobin is (b) beta barrel.2)myoglobin consists of (d…

Q: The protein pictured has .. O A) primary structure B) secondary structure C) tertiary structure D)…

A: Proteins are a class of complex nitrogen organic compounds, composed of amino acid residues joined…

Q: How many amino acids are present in this peptide? فيكم A) 6 B) 7 C) 8 D) 9

A: We have to determine the number of amino acids present in the structure below:

Q: Define the process of Drawing the Structure of a Peptide from Three-Letter Symbols ?

A: The polypeptide chain is a polymer, which is formed from the incorporation of amino acids. These…

Q: How many groups can be titrated in each pep I. R-I-C-K-E-Y II. S-M-I-L-E-Y

A: Properties of amino acids in peptides are measured by the R group and charges of the titratable…

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: Protein kinases (PTKS) are enzymes that regulate the biological activity of proteins by…

A: CELL CYCLE ❅ The process by which a parent cell divides into two daughter cells. ❅ The cell cycle…

Q: 10) Denaturation of a protein

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

Q: Identify whether each statement applies to DNA, RNA, both, or neither. A) It can contain the…

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

Q: In Protein structure: a). Write the name of the four levels of protein structure,

A: Answer of the question is below,

Q: Draw Ramachandran plot for: a) regular secondary structure with Φ = 60-65 and Ψ = 60-80

A: The combination of the backbone dihedral angles ψ and ϕ statistical distribution is shown by…

Q: The naturally occurring opioid met-enkephalin is a peptide with the structure Tyr- Gly-Gly-Phe-Met.…

A: Amino acids are zwitterions having both positive and negative charges at neutral pH. The net charge…

Q: OH

A: DNA is a long polymer of deoxyribonucleotides. Each deoxyribonucleotide is composed of deoxyribose…

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: 1) If the pH of the rain drops from 6 to 5 due to air pollution, the rain has become: a) two time…

A: Acid rain caused when the rain is mixed with the volatile toxic compounds like sulfur dioxide and…

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: Your protein has a pI of 8.34 and is in a pH 7 buffer. Which of the chromatographs below would you…

A: *Cation exchange chromatography is an ion exchange chromatography used to separate molecules based…

Q: Trypsin catalyzes the cleavage of: a) all peptide bonds b) peptide bonds after Lys or Arg c)…

A: Proteases are the enzymes that hydrolyse proteins into amino acids or peptides. They break the…

Q: It is a pyrimidine derivative that does not form part of nucleic acids.... A) Thymine B) Cytosine C)…

A: Nucleotides are the building blocks of nucleic acids. They are phosphoric acid esters of…

Q: An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b)…

A: An intermediate folding stage seen in protein denaturation or renaturation is called :and option :a)…

Q: Which of the following levels of protein structure can involve covalent bond formation? A) Primary…

A: The structure of a protein is organized into four levels of organization: primary, secondary,…

Q: Which of the following, if any, is correct about protein folding? a)2° structure formation is…

A: Protein folding is the process by which a protein molecule acquires its functional three-dimensional…

Q: The elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a…

A: Chromatography refers to the separation technique that separates substances present in a mixture.…

Q: 1) Match the nucleotide pictures to their names. A) Cytosine B) Guanine C) Thymine D) Adenine

A: An biological molecule known as a nucleotide has the fundamental building blocks of a nitrogenous…

Question

Having peptides arranged in a beta sheet would be an example of a secondary structure

A) True

B) False

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Step 3

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 3 steps

SEE SOLUTION Check out a sample Q&A here

Similar questions

What type of bonds/forces stabilize protein secondary structure? A) ionic (electrostatic) B) hydrogen bonds C) hydrophobic forces D) A and C O E) A, B and C
The following define nucleic acids EXCEPT A) They are polyionic molecules of high molecular weight composed of subunits or monomers called nucleosides. B) They are chainlike macromolecules that function in the storage and transfer of genetic information. C They are polynucleotides. They contain genes that encode for polypeptides and RNAS.
Peptide bonds cannot rotate. This is because: a) the amino acid side chains are too bulky to allow this. B) Internal hydrogen bonding hinders rotation. C) interaction with water molecules hinders rotation D) the peptide bond has considerable double bond character Polypeptide chains prefer the trans conformation. This is because: a) This distances hydrophilic groups from hydrophobic groups b) this minimizes crowding of side chains c) This brings hydrophilic groups in contact with water molecules d) This allows proteins to fold more easily Ramachandran plots indicate that protein conformation is largely a function of: a) hydrophobicity b) number of amino acids c) torsion angles d) arrangement of prosthetic groups
Which of the following statements are False? (i) Parallel b-sheets characteristically distribute hydrophobic side chains on both sides of the sheet, and antiparallel B-sheets are usually arranged with all their hydrophobic residues on one side of the sheet. (ii) Planarity of the peptide bond means that no rotation occurs about the N-Ca bond while rotation is allowed about the C(O)-N and Ca-C(O) bonds. (iii) Silk fibers consist of fibroin proteins consisting of alternating A and G or S residues. (iv) If an aspartic acid residue were present in the interior of a globular protein, it would most likely be deprotonated and thus negatively charged.
1)Ubiquitin is a small protein with a monoisotopic mass of 8560 Da. a) Electrospray ionization of this small protein typically results in major charge states of +8, +9, +10, +11, +12, and +13. Using this information, complete the table below, assuming the charges on each come from protonation. Report mass and m/z values to the ones place. b) Using the data you entered in the table, sketch an expected ESI-MS spectrum for ubiquitin. Label each peak with its charge state. What do you notice about the spacing of peaks along the x-axis. c)The figure shows an experimentally obtained electrospray mass spectrum for ubiquitin. Compare this spectrum to the spectrum you predicted. Are there any differences? If so, what might cause these differences?
O N Z—I H What is the name of the nitrogen base component of RNA shown here? ΝΗ Question 19 of 25 FO A) uracil B) guanine C) adenine D) thymine E) cytosine Submit +
Consider a short peptide with the sequence M-C-Q-L-Y-P-E-D-K. List the ionizable groups in this peptide, and the net charge of the whole peptide at pH a) 1.5, b) 7.0, and c)12.0.
Water-soluble proteins such as myoglobin tend to fold such that: A) hydrophobic amino acids R-groups are on the interior of the protein and hydrophilic groups are on the outside OB) all peptides form hydrogen bonds with water. C) hydrophilic amino acid R-groups are on the interior of the protein and hydrophobic groups are on the outside. O D) hydrophilic and hydrophobic amino acid R-groups form hydrogen bonds with each other.
Hemoglobin has two alpha-type chains and two beta-type chains. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Myoglobin has much helix-turn-helix motif. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Myoglobin folds up into a ball-like structure. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Domains differ from subunits in that: a) subunits are connected by peptide bonds while domains are not b) domains are connected by peptide bonds while subunits are not c) subunits are larger than domains d) subunits are hydrophobic while domains are hydrophilic
Give detailed Solution with explanation needed..don't give Handwritten answer....don't use Ai for answering this
Which of the following type structure contains all the three glycosphingolipids?a) B structureb) A structurec) O structured) AB structure
Indicate which of the following are present in the primary, secondary, tertiary, and quaternary structures ofproteins: a. peptidebonds b. hydrogen bonds between adjacentpeptides c. hydrogen bonds within a singlepeptide d. hydrophobic interactions e. association of four polypeptide chains