Biochemistry
8th Edition
ISBN: 9781464126109
Author: Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr., Lubert Stryer
Publisher: W. H. Freeman
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Chapter 6, Problem 10P
Interpretation Introduction
Interpretation:
Whether protein A and protein C have identical three-dimensional structures or not is to be identified.
Concept introduction:
Proteins are the
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Using Fig. as a guide, draw the complete structure of a nucleoside triphosphate before and after it becomes incorporated into a polynucleotide chain. Draw the structure that would result if the newly formed phosphodiester bond were hydrolyzed.
True or False. In a comparison between the DNAs of related organisms such as humans and mice, conserved sequences represent functionally important exons and regulatory regions, and non-conserved sequences generally represent noncoding DNA. Explain your answer in 2-3 sentences.
7 Protein structure.Circle one of the three amino acid sequences that is most likely to
form a stable a-helix?
RASKTARQ
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KPGKPAGQ
In one sentence (that can be accompanied by a small picture) explain why?
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- . Some naturally occurring polynucleotide sequences are palindromic; that is, they are self-complementary about an axis of symmetry. Such a sequence is TCAAGTCCATGGACTTGG AGTTCAGGTACCTGAACC Show how this structure might form a double hairpin, or cruciform, conformation. Indicate the center of symmetry in the sequence and the bounds of the cruciform.arrow_forwardBased. On the table explain the difference of net charge between 168.1 and the 168.10 molecular clones. Consider the initial net charge of the 168.1 clone and what ionizable amino acids contribute to such charge. Assume that histidine is neutral due to the pharrow_forwardPeptide 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_forward
- Don't copy from source.arrow_forward2. Subunit Composition of a Protein. A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography ( F). When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (=), three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein. Note: dithiothreitol is a reagent to beak down the disulfide bonds.arrow_forwardDo not give handwriting solution.arrow_forward
- help..arrow_forwardstem-loop For each of the following, identify whether it is an example of primary, secondary, or tertiary structure that might be observed in a nucleic acid (such as DNA). Answers may be used more than once. nucleotide sequence B form supercoiling kinetochore of a yeast chromosome nucleosome secondary structure primary structure secondary structure tertiary structure tertiary structure secondary structurearrow_forwardExplain well. Please . Asaparrow_forward
- This is DNA. Locate the nitrogen bases (nitrogens are blue). Where are they located in the molecule?Locate the sugars and phosphates, and describe their location. Adjacent nucleotides are linked by covalent phosphodiester bonds (-O-P-O-) produced by a condensation reaction. What parts of the adjacent nucleotides are linked by phosphodiester bonds?Two nitrogenous bases extending towards the middle of the double helix. Are there any covalent bonds between these bases?If there are no covalent bonds between these bases, what other kinds of bonds might hold the two strands of the double helix together?arrow_forwardSDS-AGE analysis of protein for subunit composition: A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography (gel filtration). When subjected to gel electrophoresis in the presence of SDS only and SDS plus 2-ME, the following pattern of SDS-PAGE is observed. MM - molecular standard proteins with known molecular weight (in kDa) as shown on the left of the gel are used to determine the size of unknown proteins. a) Determine the subunit composition of this protein (i.e., how many subunits are in its quaternary structure?). MM SDS SDS 2-ME kDa 180- 160- 100- 90- 60- 50-arrow_forwardClose contact. Examination of the structure of DNA polymerases bound to nucleotide analogs reveals that conserved residues come within van der Waals contact of C-2'C-2' of the bound nucleotide. What is the potential significance of this interaction?arrow_forward
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