Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 6.7, Problem 3CC
MAKE CONNECTIONS Ø The polypeptide chain that makes up a tight junction weaves back and forth through the membrane four times, with two extracellular loops, and one loop plus short C-terminal and N-terminal tails in the cytoplasm. Looking at Figure 5.14, what would you predict about the amino acid sequence of the tight junction protein?
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25. Your friend works in a cell biology research lab. She is working
she calls p125, because its molecular mass is 125 kiloDaltons. She knows that
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* hat do you think holds together the various secondary structural elements in a
Particular three-dimensional pattern? (Hint: Look back at Figure 4 - what is
sticking out from the sides of the a-helices and B-strands?)
glutamic acid
B
CH,
CH
valine
CH
H-N
CH
H.
valine
alanine
CH2
CH2
lysine
Figure 4-4 Essential Cell Biology 3/e (O Garland Science 2010)
Figure 6. Three examples of bonding interactions that stabilize the tertiary
structures of proteins (indicated by arrows A, B,and C). Copyright 2013 from Essential
Cell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/ Taylor &
Francis LLC.
CH2
CH,
SH
SH
CH2
CH2
OXIDATION
CH2
SH
REDUCTION
SH
CH2
CH2
Figure 4-26 Essential Cell Bialogy 3e o Garland Science 2010)
Figure 7. Disulfide bonds within proteins can form (left-pointing arrow) or be
broken (right- pointing arrow), depending on their chemical surroundings
(oxidative or reducing). Copyright 2013 from Essential Cell Biology,4th Edition by Alberts
et al.…
While investigating structure-function studies in a membrane transport protein, a researcher discovered a single nucleotide
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O AUC to GUC
GAG to CCU
GUU to GCU
GUG to UUG
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Chapter 6 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
Ch. 6.1 - Prob. 1CCCh. 6.1 - Prob. 2CCCh. 6.2 - Briefly describe the structure and function of the...Ch. 6.2 - Prob. 2CCCh. 6.3 - What role do ribosomes play in carrying out...Ch. 6.3 - Describe the molecular composition of nucleoli and...Ch. 6.3 - Prob. 3CCCh. 6.4 - Describe the structural and functional...Ch. 6.4 - Describe how transport vesicles integrate the...Ch. 6.4 - WHAT IF? Imagine a protein that functions in the...
Ch. 6.5 - Describe two characteristics shared by...Ch. 6.5 - Prob. 2CCCh. 6.5 - Prob. 3CCCh. 6.6 - Prob. 1CCCh. 6.6 - WHAT IF? Males afflicted with Kartagener's...Ch. 6.7 - In what way are the cells of plants and animals...Ch. 6.7 - Prob. 2CCCh. 6.7 - MAKE CONNECTIONS The polypeptide chain that makes...Ch. 6 - Prob. 6.1CRCh. 6 - Explain how the compartmental organization of a...Ch. 6 - Describe the relationship between the nucleus and...Ch. 6 - Describe the key role played by transport vesicles...Ch. 6 - Prob. 6.5CRCh. 6 - Describe the role of motor proteins inside the...Ch. 6 - Prob. 6.7CRCh. 6 - Which structure is not part of the endomembrane...Ch. 6 - Prob. 2TYUCh. 6 - Which of the following is present in a prokaryotic...Ch. 6 - Prob. 4TYUCh. 6 - Prob. 5TYUCh. 6 - Prob. 6TYUCh. 6 - Prob. 7TYUCh. 6 - Prob. 8TYUCh. 6 - EVOLUTION CONNECTION (a) What cell structures best...Ch. 6 - SCIENTIFIC INQUIRY Imagine protein X, destined to...Ch. 6 - WRITE ABOUT A THEME: ORGANIZATION Considering some...Ch. 6 - SYNTHESIZE YOUR KNOWLEDGE The cells in this SEM...
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- I'm honestly confused on where to start with this question. I think it has something to do with the residues per turn but can you please explain and show detailed work on the the problem. Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer. a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues that can be in each α-helixes for them to be long enough to span the bilayer? b. If one of the three α-helixes is titled at a 32° angle relative to an axis perpendicular to the surface of the lipid bilayer, what is the smaller number of amino acid helixes required for that helix to still span the lipid bilayer? c. How many hydrogen bonding interactions would there be in the smallest possible tilted transmembrane α-helix? d. If the tilted α-helix was a 310 helix instead how many amino acid residues would be required to span the lipid bilayer? How many amino acid residues would be required if…arrow_forward(c) The tube and cylinder diagram to the right illus- trates schematically the potassium channel protein from a bacterium. This channel protein consists of four identical polypeptide chains each comprised of 119 residues. The cyan ribbon illustrates only two of the polypeptide chains. The relative positions of 4 α-helices, one from each poly- peptide chain, are shown as cylinders. The red sphere in the central part of the diagram shows the position of a potas- sium ion identified by X-ray structure analysis. A cesium ion (green sphere) was also found to be stabilized in the same position when cesium chloride was introduced into the crys- tals. The cylinders each represent an α-helix running from Tyr62 to Thr74. Considering the position of the potassium ion, in- dicate on one of the cylinders at which end of the cylinder residue Tyr62 is found and at which end residue Thr74 is found. Explain the basis of your answer? Ala23 Thr119 (d) The N- and C-terminal residues of one of the…arrow_forwardProteins that span the biological membrane bilayers often contain α-helices and b-barrels. (a) Given that the insides of membranes are highly hydrophobic, predict what type of amino acyl residues would be found in a single alpha-helix that is spanning a membrane – draw a diagram to illustrate the arrangement of the R-groups within the membrane bilayer. (b) Using a drawing, illustrate the R-group arrangement in the membrane-spanning region of a channel protein for water transport if the channel was made of: six alpha-helices six beta-strandsarrow_forward
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