positive (basic), or polar negative (acidic)folded protein in the aqueous cellular environment, iswhich is responsible for major structural features of themajor property of the aminoacid side chains,theira.tertiary amine lengthb.presence of carbonsc.heptacyclic fold strengthd.formation of glycosidese.bydrophobic vs hydrophilic characterAQuestion 27 noa g to camino acids can be polar neutral, polarpositive (basic), or polar negative (aciale)a.sterolah orgo s ab.glycolicc.non-polarHydrophilice.hydrophobic

The four non-covalent interactions that stabilize the structure of a protein are: hydrophobic…

Answered: amino acids can be polar neutral, polar…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Which of the following statements is true In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood group O Lipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine
C) In biology, a very important concept is that evolution has produced organisms whose structures best perform their required function in the organism. Amazingly, this holds true for ll the levels of organization of matter from whole body parts right down to the molecules that they are made of. The function of glycogen in the body is long-term energy storage. Explain in detail how the chemical structure of glycogen corresponds to this function. aymere te heresuls of le-rancois cthesis that bre chansed. Prop 4) o bod lesinsdo to sod sdoteM viol leounlolovel" slguleov brod Iesims to sgt a) List the major differences in molecular structure between a triglyceride and a phospholipid. avel ln loss ol viq 3 16 100 10 bod obidal
Nucleic Acids Convey polypeptide c' minal directi This ques similar to t' carboxy-ter- hesis ing synth to direct sis, the Secon yase aft e genetic groups of 44. Why is ATP important to protein function, and how is it used to accomplish this? which st is. The m fatthaei, synthetic able of r ataining r thus mus ucleotid h of mor Cwas the chemis re critir a 1966 ponded han our PROT mine the s tetail sizer
tide c lirectir as ques ar to t synthr direct s, the secon aft 43. Peptide bond formation has a positive AG. What is ATP's role in making protein synthesis favorable?
Proteins involved in transport of molecules or ions into orout of cells are found in the membranes of all cells. They areclassified as transmembrane proteins because some regionsare embedded within the lipid bilayer, whereas other regionsprotrude into the cytoplasm or outside the cell. Review theclassification of amino acids based on the properties of theirR groups. What type of amino acids would you expect tofind in the regions of the proteins embedded within themembrane? What type of amino acids would you expect tofind on the surface of the regions in the cytoplasm or thatprotrude outside the cell?
29. Amino Acid Chemistry: Using the amino acid chart provided..Ala-Lys-Cys & give the isoelectric point for the tripeptide. Table 23.2 The pK, Values of Amino Acids pk, a-COOH a-NH3* Amino acid side chain Alanine 2.34 9.69 2.17 9.04 12.48 Arginine Asparagine 2.02 8.84 3.86 Aspartic acid Cysteine 2.09 9.82 1.92 10.46 8.35 Glutamic acid 2.19 9.67 4.25 Glutamine 2.17 9.13 Glycine 2.34 9.60 1.82 9.17 6.04 Histidine 2.36 9.68 Isoleucine Leucine 2.36 9.60 2.18 $ 95 10.79 Lysine 2.28 9.21 Methionine 16 9.18 Phenylalanine 1.99 10.60 Proline 2.21 9.15 Serine 2.63 9.10 Threonine 2.38 9.39 Tryptophan Tyrosine 9.11 10.07 2.20 2.32 9.62 Valine O something else! 5.14 O 8.65 something else! 5.81 9.02 9.57
Proteins that are synthesized by living organisms adopt abiologically active conformation. Yet when such moleculesare prepared in the laboratory, they usually fail to spontaneously adopt their active conformations. Can you suggestwhy?
. In glycoproteins, what are the three amino acids to whichthe carbohydrate groups are most frequently linked? Towhat functional group is the glycan linked in each case?
re aftached in a chain made rA phuephate andr A ba kleane made ef amine and eerboed gipe bee side dine iw fuckhemes ERnEEted ty hase pairs form a desle hdir. hree carboaviie neide are attached in a dyce molesale. the word(s) that best completes the statement 13. A fat that contains omly single bonds is atn) 2 fat. 14. The type of reaction that involves a single ouletaance breaking down into two Or more other substances is alu)2 seaction. 15. The energy carrier of the cell is the compound named 2 L 16. A reaction that can occur without continuing outside help is said to be 2 17. The relationship between the mass before and after a chemical reaction is described by the ? 18. Because it can proceed in either direction, the reaction between hydrogen gas and iodine gas is said to be ?. 19. An electrochemical cell that generates electricity using substances that are continually replenished from an outside source is a(n) ? cell.
A new amino acid is found with the alpha N and backbone COOH pKa's the same as histidine but with a neutral side chain. What is the isoelectric point of this new amino acid?
Residues such as valine, leucine, isoleucine, methionine, andphenylalanine are often found in the interior of proteins,whereas arginine, lysine, aspartic acid, and glutamic acid areoften found on the surface of proteins. Suggest a reason forthis observation. Where would you expect to find glutamine,glycine, and alanine?
It is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?

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