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?

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?

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

See similar textbooks

Similar questions

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?
Glycophorin, a protein in the plasma membraneof the red blood cell, normally exists as a homodimer thatis held together entirely by interactions between its trans-membrane domains. Since transmembrane domains arehydrophobic, how is it that they can associate with oneanother so specifically?
Why do some proteins require molecular chaperones to foldinto their active conformations, whereas others do not?
At pH 7, tryptophan crosses a lipid bilayer at about onethousandththe rate of indole, a closely related compound: Suggest an explanation for this observation.
Although proteins rarely if ever flip-flop across a membrane, the distribution of membrane lipids between the membrane leaflets is not absolute except for glycolipids. Why are glycosylated lipids less likely to flip-flop?
Sphingomyelins are amphipathic molecules. Review thestructure of a typical sphingomyelin. Which regions arehydrophilic and which are hydrophobic?
What type of protein structure does the active form of Catechol-oxidase most likely possess?
The cell membrane is both fluid and asymmetrical. Discuss asymmetry of the plasma membrane, as well as the enzyme involved. Explain properties that contribute to the fluidity of the cell membrane?
How is adipose tiisue matrix packed?
The protein gamma globulin has an isoelectric point of 6.60. Suppose you did a pH titration of a solution containing gamma globulin. At what pH will the protein aggregate?
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?
Chondroitin sulfate chains have been likened to a large fishnet, allowing small molecules to pass through but excluding large ones. What structural features of chondroitin sulfate and proteoglycans in general are responsible for this phenomenon?