Mechanisms of Protein FoldingQ3.2- In the Anfinsen protein folding experiment, removing urea and BMEat the same time led to functional refolding of the protein. Explain whyremoving BME without removing urea leads to a nonfunctional enzyme.Why does adding small amounts of BME alone to the solution with thenonfunctional enzyme "rescue" the function?

Anfinsen protein folding - is based on the thermodynamic protein folding hypothesis. It explain…

Answered: Q3.2- In the Anfinsen protein folding…

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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Q9
10
uestion 12 of 30 > Attempt 2 5'-GGU-3',5'-AAG-3',5'-IAC-3',5'-UGU-3', and 5'-CAA-3'. Give all A series of tRNAs have the anticodons, possible codons with which each tRNA can pair. Consider the wobble rules listed in the table. First position of anticodon C G A U I Third position of codon G U or C U A or G A, U, or C 5'-GGU-3' 5'-AAG-3' 5'-IAC-3' 5'-UGU-3' 5'-CAA-3' 3'-UUU-5' 3'-GUU-5' 3'-UUC-5' 3'-GUG-5' 3'-UUG-5' Answer Bank 3'-ACA-5' 3'-AAA-5' 3'-CUG-5' 3'-GCA-5' 3'-CCA-5' 3'-ACG-5' 3'-UGU-5' 3'-CCC-5' 3'-UCA-5' 3'-AUG-5'
rotein which How many: (a) Nitrogenous bases code for the protein? (b) Anticodons code for the protein? (c) Genes code for the protein? Identify the processes labelled 2 and 3. Indicate where process 2 takes place in a cell. Describe the process taking place at 1. Identify molecules A and B respectively. Tabulato TWO
K 2
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GQ9
A.C. 3.4 Q1. Protein synthesis is carried out by the processes of transcription and translation. A short length of DNA is shown: TACTCGTCGACGATGATC First base (a) State how many codons are present. (b) Using the table below, find the sequence of amino acids resulting from the transcription and translation of the length of DNA. Show your working. U U UUU Phenyl- UCU UUC alanine F UCC UCA -Leucine Lucc UUG-Le G CUU CUC CUA CUG A AUA -Leucine L AUU I AUC Isoleucine Methionine start codon AUG MMet GUUT GUC GUA GUG -Valine V CCU CCC CCA CCG ACU ACC ACA ACG C GCUT GCC GCA GCG Second base -Serine S -Proline P -Threonine -Alanine UAUT UAC A UAA UAG CAU CAC CAA CAG A Tyrosine Y Stop codon Stop codon -Histidine H -Glutamine AAA TAAG-Lysine AAC-Asparagine N GAU Aspartic GAC acid D GAG Glutamic G UGU-Cysteine C E UGC UGA UGG AGU AGC KAGG-Arginine CGUT CGC CGA CGG GGUT GGC GGA GGGJ Stop codon A Tryptophan -Arginine R Serine S R Glycine UCAG G SCAG SCAQ SCAG Third base
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
need good and correct answer ASAP please ??
22
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)

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