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by: Jaden Stiedemann


Jaden Stiedemann
Rice University
GPA 3.78


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Class Notes
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This 2 page Class Notes was uploaded by Jaden Stiedemann on Monday October 19, 2015. The Class Notes belongs to BIOS 201 at Rice University taught by Staff in Fall. Since its upload, it has received 18 views. For similar materials see /class/225030/bios-201-rice-university in Biological Sciences at Rice University.

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Date Created: 10/19/15
Kristina Liu S 010973 56 9208 BIOS 201 Discussion Group 4 Chaperonin Summagy Chaperones are proteins that assist in the folding and unfolding of molecules They themselves don t specify the final structure of the polypeptide but prevent polypeptide chains and subunits from aggregating into nonfunctional structures They alternate between catch and release conformations While in the catch conformation hydrophobic patches on the chaperones are revealed binding to the hydrophobic patches of the polypeptides The polypeptides folding into their tertiary and quaternary structures is then delayed The nonpolar patches are buried within the interior of the protein and the polypeptide is then released ATP hydrolysis is coupled to changes in the conformation of the chaperonin whenever ATP is bound to the chaperone it is in the catch conformation when ADP is bound the nonpolar patches on the chaperone are hidden If formin doesn t fold properly eg some hydropohobic patches are present on the polypeptide surface it is recognized by the destructive mechanisms of the cell Formin is used in the polymerization of actin This allows for the recycling of the amino acids used in the incorrectly folded protein and the removal of aberrant proteinst hat could thwart proper protein functions Different chaperones Hsp60 and Hsp70 are used so that polypeptides can get into different nooks and crannies Chaperonins only interact with the side chains of polypeptides Hsp70 is smaller than Hsp60 which is barrelshaped and consists of two rings of 7 monomers each Hsp60 is also an isolation chamber in which misfolded proteins can retry folding again The best analogy was given by Yvana who compared the process to a mom holding a kids hand Other analogies included putting ingredients into a blender and having a mixed drink pop out Kristina Dennemann 102908 Bios 201 Fall 2008 Discussion Session Group 13 Macromolecules Discussion Leader Yesle Kim Date October 29 2008 Topic Transcription complexes in eukaryotes and their functions Transcription is the process in a cell in which the genetic information stored in DNA is activated by the synthesis of complementary mRNA by enzymes called RNA polymerases Only 20 of genes are expressed in eukaryote cells and although there are many different types of protein complexes that have an effect on the transcription process in eukaryote cells only four are going to be discussed below activator complexes repressor complexes coordinately controlled genes and mediator proteins Activator complexes Transcriptional activators bind to specific DNA sequences and the chromatin context of the DNA biding site can have a positive or negative influence on binding of the activator or the proteins it recruits to the promoter Activators can bind and recruit chromatin remodeling and modifying complexes that influence the structure One function of chromatin remodeling can be to increase the stability of the activatorDNA complex and another to affect access of promoter sequences for binding of the transcription apparatus Activators also bind and recruit the transcription initiation apparatus to promoters Repressor complexes Transcriptional repressor proteins associate with their target genes either directly through a DNAbinding domain or indirectly by interacting with other DNAbound proteins A repressor protein can inhibit transcription in three selective manners by masking a transcriptional activation domain blocking interaction of an activator with other components of the transcription machinery or displacing an activator from the DNA Coordinately controlled genes Coordinater controlled genes have the same control elements and therefore respond to the same regulatory transcription factor They do not need to be near each other to function The result of this is multiple mRNA39s all made in response to the same signal They are each associated with specific regulatory DNA sequences or enhancers which are recognized by a single type of transcription factor that activates or represses a group of genes Examples of coordinate gene expression in eukaryotes include heat shock response and steroid hormone action In heat shock response exposure to high temperature activates genes coding for heat shock proteins which help stabilize and repair heat denatured proteins in the cell Steroids activate protein receptors and the proteinreceptor complex in turn activates genes In a secondary response proteins produced this way can activate another group of genes Mediator proteins Mediator proteins are a multiprotein complex that functions as a transcriptional coactivator It functions as a coactivator and binds to the Cterminal domain of RNA polymerase acting as a bridge between the enzyme and transcription factors Mutation in cells is a process that is occurred from a structure change This can occur if a protein is over expressed causing the cell division to be overstimulated or if a protein is absent and the cell cycle is not inhibited The protein complexes listed about are a few that help regulate and protect cells from this phenomena Analogies An analogy that our group came up with was a machine assembly line The assembly line emphasizes the importance of each group or part and how they must all work together to make sure the end product comes out correctly If one part slacks in timing or fails to produce the entire product will be changed mutation Applications Figuring out the mutations in cells and the mechanisms to prevent those processes would help prevent gene mutations and help treat cancer


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