Q3.2- In the Anfinsen protein folding experiment, removing urea and BME at the same time led to functional refolding of the protein. Explain why removing BME without removing urea leads to a nonfunctional enzyme. Why does adding small amounts of BME alone to the solution with the nonfunctional enzyme "rescue" the function? !

Q3.2- In the Anfinsen protein folding experiment, removing urea and BME at the same time led to functional refolding of the protein. Explain why removing BME without removing urea leads to a nonfunctional enzyme. Why does adding small amounts of BME alone to the solution with the nonfunctional enzyme "rescue" the function? !

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 3P: Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules,...

See similar textbooks

Similar questions

Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Both hsp60-like and hsp70 molecular chaperonesshare an affinity for exposed hydrophobic patches on pro-teins, using them as indicators of incomplete folding. Whydo you suppose hydrophobic patches serve as critical sig-nals for the folding status of a protein?
1CFD CALCIUM-FREE CALMODULIN How long is the protein’s primary sequence?Does this protein have any secondary, tertiary and/or quaternary structures present?Are there any molecular additions to this protein that are not amino ac
a) Canonical forces in protein folding. Describe how these forces come into play when a protein folds. Why do are other intermolecular interactions important to fully understand folding processes?
SDS-AGE analysis of protein for subunit composition: A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography (gel filtration). When subjected to gel electrophoresis in the presence of SDS only and SDS plus 2-ME, the following pattern of SDS-PAGE is observed. MM - molecular standard proteins with known molecular weight (in kDa) as shown on the left of the gel are used to determine the size of unknown proteins. a) Determine the subunit composition of this protein (i.e., how many subunits are in its quaternary structure?). MM SDS SDS 2-ME kDa 180- 160- 100- 90- 60- 50-
Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?
Explain what the meaning of these distances is (e.g., from where to where?)Crystal structure of human monocyte chemotactic protein-2
.A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little if any effect from adding
Which statements are true? Explain why or why not.1 Each strand in a β sheet is a helix with two aminoacids per turn.2 Intrinsically disordered regions of proteins can beidentified using bioinformatic methods to search genes forencoded amino acid sequences that possess high hydro-phobicity and low net charge.3 Loops of polypeptide that protrude from the sur-face of a protein often form the binding sites for other mol-ecules.4 An enzyme reaches a maximum rate at high sub-strate concentration because it has a fixed number ofactive sites where substrate binds.5 Higher concentrations of enzyme give rise to ahigher turnover number.6 Enzymes that undergo cooperative allosteric tran-sitions invariably consist of symmetric assemblies of mul-tiple subunits.7 Continual addition and removal of phosphatesby protein kinases and protein phosphatases is wastefulof energy—since their combined action consumes ATP—but it is a necessary consequence of effective regulation byphosphorylation.
Loop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the roles
Part C Using the values of pKas in the table below, calculate the pI for DTLH. Properties of some amino acids found in proteins Name Aspartic acid Abbreviations: 1- and 3- letter codes D, Asp Histidine H, His Leucine L, Leu Threonine T, Thr ΓΙ ΑΣΦ Submit pKa of a-COOH pKa of a-NH3+ pKa of lonizing Group Group Side Chain Express your answer to two significant figures. Request Answer 2.1 1.8 2.4 2.6 ? 9.8 9.2 9.6 10.4 3.9 6.0
estion 2 Using the Chou-Fasman rules (without calculating numerical probability) predict the secondary structural elements in the following protein sequence. Give the residue numbers or residue range and state the secondary structure. Arg- Pro-Glu- Lys-Val-Thr-Trp-Tyr-Phe-lle Arg-Arg-Asn-Pro-Gly-Asp-Arg 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16. 17 For the toolbar, press ALT+F10 (PO) or ALT+RN+F10 (Mac)