Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 2, Problem 2P
Draw two different possible hydrogen-bonding interactions between two molecules of formamide (HCONH2). Clearly label the hydrogen-bond donor and acceptor atoms. Which of these two possible hydrogen-bonding interactions is more likely to occur? (Hint: Consider resonance structures for formamide.)
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
Identify the potential hydrogen bond donors and acceptors in the followingmolecules:
What is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0
and (c) 7.0? CLUE: draw the structure of lysine and show its different charged forms; then
consider in which pH domains the pKa values for deprotonation/protonation occur.
With the aid of a simple generic diagram:
i) IDENTIFY and EXPLAIN how the type(s) of chemical bonding stabilizes a SECONDARY structure that is present in 3GRS(Glutathione Reductase)??? https://www.rcsb.org/
ii) Describe why position 58 (Cysteine ) in 3GRS is important ???
and outline the
Effects of the mutation from Cysteine 58 (Cys) to Glycine(GLY) will have on the 3D structure??
Effect of the mutation from Cysteine 58 (Cys) to Glycine (Gly )will have on the function of 3GRS??
I am stuck! please help only correct answers pls!
Chapter 2 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 2 - Suppose a chloride ion and a sodium ion are...Ch. 2 - Draw two different possible hydrogen-bonding...Ch. 2 - Prob. 3PCh. 2 - 4. What is the pH of each of the following...Ch. 2 - Prob. 5PCh. 2 - The weak acid HA is 2% ionized (dissociated) in a...Ch. 2 - 7. Calculate the pH values and draw the titration...Ch. 2 - What is the pH of the following buffer mixtures?...Ch. 2 - a. Suppose you wanted to make a buffer of exactly...Ch. 2 - Prob. 10P
Ch. 2 - You need to make a buffer whose pH is 7.0, and you...Ch. 2 - Describe the preparation of 2.00 L of 100 glycine...Ch. 2 - Carbon dioxide is dissolved in blood (pH 7.4) to...Ch. 2 - What is the molecular basis for the observation...Ch. 2 - The anno acid arginine ionizes according to the...Ch. 2 - It is possible to make a buffer that functions...Ch. 2 - A student is carrying out a biological preparation...Ch. 2 - Histidine is an amino acid with three titratable...Ch. 2 - Prob. 19PCh. 2 - A biochemical reaction takes place in a 1.00 ml...Ch. 2 - Is RNA-binding enzyme RNase A more likely to have...Ch. 2 - Consider a protein in which a negatively charged...Ch. 2 - Prob. 23PCh. 2 - Prob. 24P
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- An oligopeptide has the following amino acid sequence: NH2-Ala-Glu–Leu–Trp–Tyr-Ser–Gly–Lys–Leu-Ala–Arg-Ala-Phe-Ile-Pro–Gly-COOH a) Estimate the net electric charge of the molecule at pH 8.0 and pH 11.0. b) If the above peptide is passed through a cation exchange chromatographic column (that is, the matrix of the column has negative charges) stabilized at pH 8.0, would you expect it to be retained on the column? c) Indicates the number of fragments, and the sequence of each of them, that would be obtained when treating the peptide in question with: i) trypsin, ii) chymotrypsin.arrow_forwardDetermine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at: a. pH 1.0 b. pH 10.1arrow_forwardConsider the following fatty acid attached below. a) What is the number convention for this fatty acid above, including the location of the double bond from the α carbon end? Remember to use the Δ (delta) in your answer for the double bond location b) What is the ω (omega) numbering of the double bond for the fatty acid above? c) What is the product after two hypothetical additional rounds of synthesis for the fatty acid? Remember that synthesis adds 2 carbons at a time to the carboxylic end.arrow_forward
- With the aid of the simple generic diagram, identify and explain how the type of chemical bonding stabilizes a secondary structure present in 3GRS (glutathione reductase).arrow_forward(a) A decapeptide has the following amino acid composition: Alaz, Arg, Cys, Glu, Gly, Leu, Lys, Phe, Val Partial hydrolysis yields the following tripeptides: Cys-Glu-Leu + Gly-Arg-Cys + Leu-Ala-Ala+ Lys-Val-Phe + Val-Phe-Gly. Reaction of the decapeptide with 2,4-dinitrofluorobenzene yields 2,4-dinitrophenylysine om the experimental data, deduce the primary structure of the decapeptide.arrow_forwardA NONAPEPTIDE that attacks and kills cancer cells has just been recently isolated from a rare fungus. Amino acid analysis of the peptide reveals the following information below: (NOTE: when the sequence is not known, a comma separates the amino acids) Hydrazine Acid Hydrolysis (6 N HCI) at 110 "C Nonapeptide (2) Arg, Gln, (2) Tyr, Gly, Ser, Thr, and Met 2,4-dinitrofluorobenzene DNP-Thr Gin and modified free Peptide 1 (Arg, Thr, Ser) amino acids Cleavage with Trypsin, then chromatography Peptide 2 (Gly, Tyr, Arg) Met Tripeptide Cyanogen bromide Dipeptide Peptide 3 (Arg, Ser, Tyr, Thr) Cleavage with Chymotrypsin, then chromatography Amino acid Peptide 4 (Gly, Arg, Tyr)arrow_forward
- The key reaction steps in the Edman degradation of polypeptides, which removes the N-terminal amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the expected outcome if the N-terminal amino acid is proline (Pro)? (The structure of proline is provided below for your reference.) NH-C00 NH CO0 phenyl isothiocyanate PITC NH CO0 NH CO0 peptide without the thiszolinone original Nterminal amino acid HE a PTH-amino acid Proline: HN HN. O Edman's reagent will not react with an N-terminal proline.arrow_forwardDraw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone geometry (all angles +/- 180°). Include correct stereochemistry for L-amino acids. Label all bond rotations representing the angles at each residuearrow_forwardFor the following amino acids select the INCORRECT alternative: (a) At pH = 4 all migrate towards the cathode except Asp. (b) At pH = 10 all migrate towards the anode. (c) The pI of phenylalanine (Phe) will be about 5.5. (d) The pl of aspartic acid (Asp) will be about 2.8. (e) At pH = 7 the amino acids Arg and Lys migrate towards the cathode and the rest to the anode.arrow_forward
- One or more of the compounds shown below will satisfy each of the following statements. Not all compounds may be used; some may be used twice. Put the number(s) in the blank. (1) Found in chitin. (2) An L-saccharide. (3) The first residue attached to asparagine in N-linked glycans. (4) A uronic acid. (5) A ketose. CH,OH CoO COO OH H H H H ОН Н но OH OH H OH H HO OH H NHC- CH, Oso, OH (a) (b) (c) CH,OH CH,OH CH,OH C=0 CHOH C=0 H-C- OH CH,OH но -с-н ČH,OH CH,OH (d) (e)arrow_forwardDraw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in acqueous solution at pH=10.3. (Relevant pKa values are: 2.2,4.3,6.0,9.8 and 10.1)arrow_forwardEach 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.(a) Histidine has three ionizable functional groups. Write the equilibrium equations for its three ionizations and assign the proper pKafor each ionization. Draw the structure of histidine in each ionization state. What is the net charge on the histidine molecule in each ionization state?(b) Draw the structures of the predominant ionization state of histidine at pH 1, 4, 8, and 12. Note that the ionization state can be approximated by treating each ionizable group independently.(c) What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate toward the anode (+) or cathode (−) when placed in an electric field?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. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals 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 Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals 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
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license