Classify each characteristic as describing glycoproteins or proteoglycans.GlycoproteinsProteoglycansAnswer Bankform highly specific sites for recognitiononly has sulfated glycosaminoglycan chainsfound in Golgi complexes, secretory granules,and high-affinity binding by lectinscovalently linked to Serand lysosomesexclusively located at the cell surfacemay contain N-linked glycosidic bondsinclude the heparan sulfate familyand in the extracellular matrix

Those molecules that structure and perform various functions in the living body are referred to as…

Answered: Classify each characteristic as…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter32: The Reception And Transmission Of Extracellular Information

Section: Chapter Questions

Problem 11P

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If the RGD tripeptide sequence in fibronevtin wete absent. Which is true? integrims would not bind to fibronectin cadherins on adjacent cells would not be able to interact in a homotypic fashion. fibronectin could not form crosslink with other extracellular matrix proteins. glycosaminoglycans would not be able to assemble onto proteoglycans.
The glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?
Treatment of a polypeptide with 2-mercaptoethanol yields two polypeptides 1. Ile—Val—Cys—Arg—Thr—Gly—Cys—Lys—Asn—Phe—Leu2. Trp—Lys—Cys—Phe—Arg—His—Thr—Lys—Cys—SerTreatment of the intact polypeptide with trypsin yields fragments with the following aminoacid compositions(Arg, Cys2, Ile, Ser, Val)(Arg, Cys2, Gly, Lys, Thr, Phe)(Asn, Leu, Phe)(His, Lys, Thr)(Lys, Trp)Edmands chemistry reveal the following PTH derivatives in equal quantity after cycle 1• PTH--Ile and PTH--Trp a) Rewrite the intact polypeptide, by indicating the positions of the disulfide bonds(Indicate your reasoning) b) How many products do you expect after chymotrypsin cleavage of the intactpolypeptide? c) You are performing an isoelectric focusing experiment (IEF) on a gel with a pH range of 2to 14. Indicate on the diagram below at what point along the gel will peptide 1 abovefocus, in the presence (X) and absence (Y) of DTT. (also show your calculations)
Proteoglycan aggregates in tissues form hydrated, viscousgels. Can you think of any obvious mechanical reason whytheir capacity to form gels is important to cell function?[Hint: Liquid water is virtually incompressible.]
provide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)
Classify the fold of each protein. Classify the fold of each domain asall a (or mostly a), all b (or mostly b), a/b, or a+b.. 1. Firmicute collagen-binding protein (1FCB): 2. Bat glycosyltransferase (2BGT): 3. Proteobacterial nitrite sensor (3PNS):
erioiogy e cell walls of Gram-positive and Gram-negative bacteria are structurally different but both contain peptidoglycan. Which TWO of the following statements about peptidoglycan biosynthesis are CORRECT? O Peptidoglycans are made from alternating units of N-acetylmuramic acid and N-acetylglucosamine. O N-acetylglucosamine is synthesised from N-acetylmuramic acid by the addition of acetic acid derived from phosphoenolpyruvate. O Peptidoglycan synthesis in Gram-positive bacteria involves the addition of the amino acids, L-alanine, D-glutamic acid, L-lysine, to N-acetylmuramic acid. O D-glutamic acid-D-glutamic acid dipeptide is linked to the tripeptide side chain of N-acetylmuramic acid to form N-acetylmuramic acid-pentapeptide O At the beginning of the biosynthesis pathway, the N-acetylglucosamine-N-acetylmuramic acid-pentapeptide-phospholipid crosses the cell membrane and is added to growing peptidoglycan chain. O The transglycosylase enzyme is located on the inner face of the…
Disulfide bond formation is a regularly observed protien modification that occurs in the lumen of the ER. Explain why disulfifde bond formation is a modification only found in secretory proteins and the extracellular domain of plasma membrane proteins. Furthermore, highlight the advantages disulfide bonds provide to these proteins.
Using the ActiveModel for phosphofructokinase (Trypanosoma), describe the difference between the APO1, AP02, and holoenzyme conformations.
HC CH reaction with HC CH lysosome CH CH HC CH3 HC CH3 HC CH HC. CH CH3 CH3 ОН OH inside the cell, propranolol sometimes encounters lysosomes, which alter its NH group as shown above (right). reacting with the lysosomes, propranolol becomes trapped inside the cell and can cause psoriasis or other inflammatory side effects. Use IMFS to explain why the altered propranolol gets trapped. T
The amino acid sequence Leu-His-Arg-Leu-Asp-Ala-Gln-SerLys-Leu-Ser-Ser is a signal sequence that directs proteinstowards the endoplasmic reticulum, say if it is true or false if it is false justify it.
Which describes the enzymatic activity/biochemical function of dynamin? Answers: bind to and (quickly) hydrolyze GTP for energy while pinching off vesicles from a donor membrane surface in collaboration with clathrin bind to signal sequences in nascent secretory proteins, the ribosome, and to the SRP receptor, bind to and (slowly) hydrolyze GTP when the ribosome is bound to the translocon bind to nuclear localization sequences and to importin-beta bind to and (slowly) hydrolyze GTP while recruiting (binding to) vesicle coat proteins

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