Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Question
Chapter 2, Problem 19P
Interpretation Introduction
Interpretation:
The reason for loops on the proteins to be composed of number of hydrophilic amino acids needs to be explained.
Concept introduction:
The proteins are made up of amino acids joined together. Therefore, amino acids are like building blocks for them. The proteins play an important role in all the biological processes. A huge proportion of our cells, tissue and muscles are made up of the amino acids. Thus, they carry out several significant functions in the body.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Need help.
Which one of the following statements is FALSE?
Group of answer choices
A.Beta-pleated sheets are part of the secondary structure of proteins
B.The nitrogenous bases of DNA are located on the inside because they are hydrophobic in character
C.The peptide bond is formed by dehydration synthesis
D.Alpha helices are stabilized by attraction between the amino acid R groups
E.The peptide bond is rigid and planar and has partial double bond character
Sweet proteins. List the key classes of glycoproteins, their defining characteristics, and their biological functions.
Be sure to answer all parts.
Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv),
Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl:
Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.
Chapter 2 Solutions
Biochemistry
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
Knowledge Booster
Similar questions
- V-A. Which of the following amino acids will elute first in a cation-exchange column using a buffer at pH 7? 1. Asp or Lys 2. Arg or Met 3. Gly or Val 4. Ser or Alaarrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Lys, Pro, Tyr, Ile (2 equiv) , Gln, Trp, Phe, and forms the following fragments when partially hydrolyzed with HCl: Lys–Ile-Phe-Pro, Phe-Pro-Gln-Tyr, and Trp-Ile-Lys.arrow_forwardBe sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Val, Met, Asp (2 equiv), Phe, Trp, Ile, Lys, and forms the following fragments when partially hydrolyzed with HCl: Ile-Asp-Phe, Lys-Met-Val-Trp, and Phe-Asp-Lys-Met. Trp Leu Phe Leu Val Lys Gly Tyr Xarrow_forward
- The power of proteins. Discuss how proteins can cause disease, and be used to diagnose and treat diseases.arrow_forwardPeptides. 1. Draw the peptide Ala-Glu-Gly-Lys, as it would occur at physiological pH = 7.4. The R groups of Ala and Gly are not acidic or basic, therefore do not have a pka and the charge on these R groups is therefore independent of pH. Glu is acidic and Lys is basic, therefore the charge on these amino acids is pH dependent. The pKas are shown below. pKa N-term = 9.0 C-term = 3.5 Glu4.1 Lys = 10.5 2. Draw a circle around the peptide bonds. 3. Label the C-terminus and the N-terminus. 4. What is the overall charge on the peptide at pH 7.4?arrow_forwardNeed help. (a) Two ligands bind to the same site of a protein. However, when examined by ITC, for one of the ligands heat needs to be added to the system to maintain constant temperature, whereas for the other ligand, heat must be removed. Why is this the case?arrow_forward
- Beta folding. Parallel and antiparallel beta folding sheets (be able to draw). Beta loops. Examples of proteins formed mainly by this structure.arrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Catalase with H2N-...KERINGKERIANGEKSAMSKL-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? (specify the compartment) What is the name of the specific receptor of this polypeptide? The receptor may also have what alternative function?arrow_forwardAccepting. Which of the following compounds readily accepts amino groups from amino acids? a. Glutamine b. Isocitrate c. Malate d. a-Ketoglutarate-Ketoglutaratearrow_forward
- 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?arrow_forwardtrue 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.arrow_forwardSIGNALS AND TARGETS. Listed below are sample polypeptides/proteins with their signal molecule/peptide. Answer the questions that follow. If you are asked to give the amino acid sequence, provide the sequence using the three-letter names of the amino acids (eg. ser-ala-met). Polymerase with H2N-...GMMTVPPKKKRVGMMTV...-COOH Provide the amino acid sequence of the signal peptide Where will this polypeptide be transported? What is the receptor of the signal sequence? What is the transport complex for this protein?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON