Concept explainers
QUANTITATIVE That’s About the Size of It. From chemistry, we know that each methylene (—CH2—) group in a straight-chain hydrocarbon advances the chain length by about 0.13 nm. And from studies of protein structure, we know that one turn of an α helix includes 3.6 amino acid residues and extends the long axis of the helix by about 0.56 nm. Use this information to answer the following.
(a) How long is a single molecule of palmitate (16 carbon atoms) in its fully extended form? What about molecules of laurate (12 C) and arachidate (20 C)?
(b) How does the thickness of the hydrophobic interior of a typical membrane compare with the length of two palmitate molecules laid end to end? What about two molecules of laurate or arachidate?
(c) Approximately how many amino acids must a helical transmembrane segment of an integral membrane protein have if the segment is to span the lipid bilayer defined by two palmitate molecules laid end to end?
(d) The protein bacteriorhodopsin has 248 amino acids and seven transmembrane segments. Approximately what portion of the amino acids are part of the transmembrane segments? Assuming that most of the remaining amino acids are present in the hydrophilic loops linking the transmembrane segments together, approximately how many amino acids are present in each of these loops, on average?
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Becker's World of the Cell (9th Edition)
- . Pick all that are TRUE regarding analysis of quaternary structures of proteins using polyacrylamide electrophoresis:I. The added β-mercaptoethanol disrupts S--S bonds bridging the polypeptide chains causing the appearance of higher Rf bands compared to the native protein run. II. Heating up any protein before subjecting to SDS-PAGE will always result in the formation of more than one band.III. A good asymmetrical gel layout would be : (Lane 1) MW ladder, (2) native protein, (3) protein + β-ME, (4) protein + HCL, (5) protein + β-ME + HCl.IV. Formation of a single band in the protein + β-ME + HCl run, whose Rf is lower than the native run, could be indicative that the protein is a homodimer.A. I onlyB. I and IIC. II and IIVD. None is truearrow_forwardGiven a peptide chain that is composed of the following amino acids:(branched chain-- polar uncharged--polar positively charged -- polar negatively charged-- aromatic) 10If the component amino acids of the above peptide chain are subjected to paper chromatography, which of the amino acids will be farthest from the point of origin?arrow_forwardE. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o oarrow_forward
- Beta-carotene is red-orange pigment abundant in plants and fruits. Assuming that it can be modeled as a particle in a 1-D box, estimate how long the red-conjugated chain is given that A = 475 nm in hexane.' Using an average conjugated CC bond length of 140 pm, how long should the "box" be? Figure 1. Beta carotene %3Darrow_forwardImagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. Here's what R looks like: -CH- CH HO CH O yes Could R, form a salt bridge with R, at physiological pH, if R₂ were the right kind of residue? O no If you said R, could form a salt bridge with R₂, what would R, have to be? If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the 3-letter code of any of them. Explanation Check Z X E all option H cmd H N J 0 O P cmd optionarrow_forward. Give two reasons to explain why a proline residue in the middle of an ahelix is predicted to be destabilizing to the helical structurearrow_forward
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- draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 and put each charges beside the amino acids then compute for the isoelectric point please show complete solution DEHINSarrow_forwardPlease don't copy Chemistry All of the following tend to favor a helical conformation of a single polynucleotide chain EXCEPT: Group of answer choices A. hydrophobic interactions of the rings of the purine and pyrimidine bases that exclude water. B. charge–charge repulsion of phosphate residues of the polynucleotide backbone. C. hydrogen bonding between appropriate purine–pyrimidine pairs. D. interchange of electrons in the p orbitals of the purine and pyrimidine bases.arrow_forwardChemistry The soybean-like plants on planet 20170113 also have a globular heme-containing protein made of alpha helices. The last helix has the sequence Phe-Glu-Ala-Gln-Leu-Lys-Asn-Arg-lle- Ser. How many full turns are in this helix? 01 02 03 Oarrow_forward
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