18The image below shows the different interactions responsible for the spontaneous folding of a protein molecule. Identify which interactions are involved for each labelledregion0-HHCH,OHCH,NH,0BO-H--OOCH,CH₂ABDCAयह महCHCH₂COOHCHCH,CH,CH,CHH--O=CDT(CHJANH,- interactionsion-dipole interactionHydrogen bondingHydrophobic interactionsDisulfide bondslon-ion interaction18

According to Anfinsen's hypothesis the sequence or primary structure of a protein f=determines the…

Answered: The image below shows the different…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter3: Biological Macromolecules

Section: Chapter Questions

Problem 2VCQ: Figure 3.23 Which categories of amino acid would you expect to find on the surface of a soluble...

See similar textbooks

Similar questions

Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
Define the following terms:a. salt bridgeb. oligomerc. allosteric transitiond. protein denaturatione. amphipathic molecule
Please Answer numbers 1, 2 & 3 thank you 1. Which of the following intermolecular molecular forces of attraction is disrupted when a native protein is added with acetic acid? a. Hydrogen bond b. Peptide bond c. Disulfide bond d. Salt bridge e. van der Waals force 2. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Phe-Met-Cys- which of the following test will the sample be positive? a. Lead-sulfide test b. Hopkins cole's test c. Millon's test d. Xanthoproteic test 3. Suppose a protein sample with a fragment containing the following amino acid sequence is subjected to various chemical assay/tests. - Ala-Gly-Trp-Phe-Met-Cys- What is observed when the protein sample is subjected to Millon’s test? a. Violet interface b. Red precipitate/solution c. Brown/black precipitate d. Yelllow product e. No observable result
Indicate the level(s) of protein structure to which each of thefollowing contributes:a. amino acid sequenceb. b-pleated sheetc. hydrogen bondd. disulfide bond
In the tertiary structure of a protein, which pair of amino acid side chains would be most likely to participate in hydrophobic interactions? Asn/lys ser/cys gln/tyr val/thr phe/lêu
Which of the following statements are correct about the molten globular state of protein folding (select all that appy)? A. May be short-lived or long-lived intermediate in protein folding B. Contains substantial levels of secondary structure C. Has loose packing of hydrophobic core D. Larger radius of gyration than dentaured state E. Is a more compact state than the native confomation
Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the above
Although all of these may play a part, the major driving force in protein folding is: a) hydrogen bond formation b) salt bridge formation c) steric interactions d) the hydrophobic effect A partially folded protein is called a a) peptide template b) active domain c) molten globule d) precursor protein Which of these processed is NOT seen in protein denaturation? A) subunits are dissociated b) folding is unraveled c) alpha helix and beta sheets are unraveled d) peptide bonds are broken. A protein which has more than one stable conformation is called a: a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein If a denatured protein does not spontaneously renature upon removal of denaturing agents, it may require a ____ to renature. a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein Prion protein and amyloid protein have which trait in common? A) They denature very easily…
a) In the article the authors reference the canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do the authors suggest that other intermolecular interactions must be important to fully understand folding processes? https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6995338/pdf/nihms-1067149.pdf
Which of the following statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acids
Which of the following statements are correct about the thermodynamics of protein folding (select all that appy)? A. The deltaG for protein folding is negative B. Burial of hydrophobic side provides a positive entropy change that drive protein folding C. The overall entropy change of protein folding is favorable D. Intercations between amino acids provide a large negative deltaH that helps favor the native state. E. The free energy change of protein folding is dependent on the temperature
Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – Cterm

SEE MORE QUESTIONS

Recommended textbooks for you

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

SEE MORE TEXTBOOKS