ORGANIC CHEM W/BIOLOGICAL TOP. ACCESS
6th Edition
ISBN: 9781264382545
Author: SMITH
Publisher: MCG CUSTOM
expand_more
expand_more
format_list_bulleted
Videos
Textbook Question
Chapter 3, Problem 41P
Intramolecular force of attraction are often important in holding large molecule together. For example, some proteins fold into compact, held together by attractive forces between nearby
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
10) The a helix of the secondary structure of a protein is held together by hydrogen bonds between two different
parts of a protein chain.
True or False
1) Hydrophobic interactions help to stabilize the tertiary and quaternary structures of a protein.
True or False
Chamistry
4. The figure below is a cartoon
representation of a large biomolecule called a
peptide, made up of different types of amino
acids. Near the bottom of the figure are two
chemical groups that are part of different
amino acids in different positions along the
chain. Based on the structures of those
groups, what type of force is represented by
the dashed red line? Be sure to consider any
charges that are shown.
E Amino
Acids
Palbpeptide Chain
Chapter 3 Solutions
ORGANIC CHEM W/BIOLOGICAL TOP. ACCESS
Ch. 3.1 - Prob. 1PCh. 3.2 - (a) Classify the carbon atoms in each compound as...Ch. 3.2 - Problem 3.3 Classify a carbon atom by the number...Ch. 3.2 - Classify each alkyl halide and alcohol as , or...Ch. 3.2 - Prob. 5PCh. 3.2 - Prob. 6PCh. 3.2 - Draw the structure of a compound of molecular...Ch. 3.2 - Prob. 8PCh. 3.2 - Prob. 9PCh. 3.2 - Draw the structure of a compound fitting each...
Ch. 3.4 - Predict which compound in each pair has the higher...Ch. 3.4 - Prob. 17PCh. 3.4 - a Label the hydrophobic and hydrophilic portions...Ch. 3.5 - Prob. 21PCh. 3 - 3.29
Identify the functional groups in the...Ch. 3 - Prob. 32PCh. 3 - 3.31 For each alkane: (a) classify each carbon...Ch. 3 - 3.32 Identify the functional groups in each...Ch. 3 - 3.33 Identify each functional group located in the...Ch. 3 - 3.34 (a)Identify the functional groups in...Ch. 3 - Draw seven constitutional isomers with molecular...Ch. 3 - Prob. 38PCh. 3 - Prob. 39PCh. 3 - Prob. 40PCh. 3 - Intramolecular force of attraction are often...Ch. 3 - 3.40 (a) Draw four compounds with molecular...Ch. 3 - 3.41 Rank the compounds in each group in order of...Ch. 3 - Explain why CH3CH2NHCH3 has higher boiling point...Ch. 3 - Prob. 45PCh. 3 - 3.44 Rank the following compounds in order of...Ch. 3 - Prob. 47PCh. 3 - 3.50 Predict the solubility of each of the...Ch. 3 - Prob. 52PCh. 3 - Prob. 53PCh. 3 - 3.53 THC is the active component in marijuana, and...Ch. 3 - Prob. 55PCh. 3 - Prob. 56PCh. 3 - 3.60 Quinapril (trade name Accupril) is a drug...Ch. 3 - 3.61 Answer each question about oxycodone, a...Ch. 3 - Prob. 65PCh. 3 - Prob. 66PCh. 3 - 3.64 Explain why A is less water soluble than B,...Ch. 3 - 3.65 Recall from section 1.10B that there is...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- . How many unique amino acid sequences are possible for a tripeptide containing only the amino acids gly, ala, and cys, with each amino acid occurring only once in each molecule?arrow_forwardDraw a segment of the backbone of a protein that is long enough for three peptide linkages to be present.arrow_forwardAlthough RNA is single-stranded, the strand sometimes folds back on itself to give a complementary portion. What would be the complementary portion of the RNA fragment having the bases uracil-cytosine-guanine? A virus is a particle that contains DNA or RNA that is surrounded by a coat of protein that can replicate only in a host cell. The influencza virus shown in this electron microscope image is an RNA virus.arrow_forward
- Which of the following is the primary driving force in the folding of a protein? a) The increase in entropy of the protein as it shifts to the final folded structure. b) The formation of stabilizing hydrogen bonds in the secondary structures. c) The formation of stabilizing disulfide bonds. d) The increase in entropy of the surrounding water as the protein folds e) The association of dipole/dipole interactions among charged amino acidsarrow_forwardHow do amino acids bond together ? Use a basic diagram of an amino acid molecule ato show how 2 amino acids would bond together. Identify the ty of reaction as well the type of bond formed.arrow_forwardLabel the molecular shape around each of the central atoms in the amino acid glycine. You are currently in a labeling module. Turn off browse mode or quick nav, Tab to items, Space or Enter to pick up, Tab to move, Space or Enter to drop. trigonal pyramidalmulti-use tetrahedralmulti-use trigonal planarmulti-use bentmulti-use Answer Bank tetrahedralmulti-use linearmulti-use trigonal planarmulti-use trigonal pyramidalmulti-use bentmulti-usearrow_forward
- As we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected. b) Another observation is that although the N-H of the peptide bond is able to serve as a H-bond donor the N atom of the peptide bond does not serve as an effective H-bond acceptor. Provide an explanation for this observation, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.c) It is also fairly accepted that while proteins undergo dynamic motions and conformational changes, and while R groups can freely rotate about Cα, it is generally not possible to freely rotate around a peptide bond. Please explain this observation, using a picture showing relevant orbitals on relevant atoms (your answer for part (a) might provide a useful basis for your reasoning…arrow_forwardzy Section 41.26 - COMP B11: Programming Concepts and Methodology I Syllabus Scores eText Document Sharing User Settings Course Tools > Cholesterol belongs to the steroid class of lipids because it contains a multiring structure known as a steroid nucleus. Cholesterol is also classified as a sterol because it contains a hydroxyl group on the third carbon atom of the steroid nucleus. The structure of cholesterol is shown below. (Figure 1) Cholesterol can be obtained from food, but most is synthesized by the body. Cholesterol is an important component of many structures in the body, including cell membranes, nervous tissue, skin, and the liver. Figure HO CH3 CH3. CH3 Cholesterol 1 of 1 CH3 CH3 openvellum.ecollege.com MyLab and Mastering Q Q E Course Home Select the carbon atoms of the steroid nucleus in the molecule of cholesterol shown. Note that the hydrogen atoms have been omitted for clarity. P Pearson Review | Constants | Periodic Table Identify the appropriate group of atoms by…arrow_forward8) Which R group would most likely be found in a hydrophobic area of the tertiary structure of a protein? A) -CH2OH B) -CH2COO- C) -CH2 D) -CH2CH2CH2CH2 N H3arrow_forward
- Am I correct? Please helparrow_forwardAs we’ve discussed, a peptide bond is made when amino group of one amino acid combines with the carboxylic acid group of another amino acid (releasing a water molecule in the process). The C-N bond formed in this process is called a peptide bond. Peptide bonds have a few properties that might be unexpected. a) One property is that the molecular geometries around the C and N atom in the peptide bond are generally planar with bond angles of approximately 120 degrees. Provide an explanation for why the peptide bond would have this property, using Lewis structures, VSEPR theory and/or valence bond theory as appropriate.arrow_forwardPart C: Amino Acids Amino Model/Polarity Lewis Structure Zwitterion Acid Model Alanine Polarity Model Serine Polarity Model Glutamic Polarity Acid Model Polarity Lysinearrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Chemistry: Matter and ChangeChemistryISBN:9780078746376Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl WistromPublisher:Glencoe/McGraw-Hill School Pub Co
ChemistryChemistryISBN:9781305957404Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCostePublisher:Cengage Learning
Chemistry: An Atoms First ApproachChemistryISBN:9781305079243Author:Steven S. Zumdahl, Susan A. ZumdahlPublisher:Cengage Learning
General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,
Chemistry: Matter and Change
Chemistry
ISBN:9780078746376
Author:Dinah Zike, Laurel Dingrando, Nicholas Hainen, Cheryl Wistrom
Publisher:Glencoe/McGraw-Hill School Pub Co
Chemistry
Chemistry
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Cengage Learning
Chemistry: An Atoms First Approach
Chemistry
ISBN:9781305079243
Author:Steven S. Zumdahl, Susan A. Zumdahl
Publisher:Cengage Learning
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
07 Physical Properties of Organic Compounds; Author: Mindset;https://www.youtube.com/watch?v=UjlSgwq4w6U;License: Standard YouTube License, CC-BY