For a protein containing no -sheet secondary structure the CD spectrum gives[0] 222 = -29,750 deg.cm ?.decimole 1. Given from reference spectra that 100% helix has a[e] 222 = -36,000 deg.cm ?.decimole and 100% coil has a [0] 222 = +3,000 deg.cm 2.decimole 1a). What is the percentage alpha helical content of the protein? Show your working.b.) The protein and a short duplex oligonucleotide are added at equimolar concentration in abuffer containing 100 mM NaCl and then in a buffer containing 1 M NACI, the two samplesare analysed by CD. The spectra in the 250 to 280 nm region differs considerably betweenthe samples but the spectrums in the 200 – 230 nm range are similar. What hypothesis canyou form concerning the protein?

Circular dichroism is a spectroscopic technique to find out the secondary structure, folding and…

Answered: a). What is the percentage alpha…

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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Similar questions

Protein a will fold into its native state only when protein b is also present in the solution however protein b can fold itself into native confirmation without the presence of protein a which of the following is true
a) The pl of a protein is 9.0. What will be the net charge (positive, negative or neutral) on the protein under the following conditions: A buffer with pH 9.0: A buffer with pH 7.0: A buffer with pH 10.0: b) Your protein is present in a sample buffer which has a pH 7.0. The sample is applied to an ANION EXCHANGE column. Will protein 1 bind to the beads on the column? Yes/No
You ran a gel using SDS-PAGE. Total molecular mass of your unknown protein (determined via gel filtration): 217 kDa Standard curve equation based on your protein ladder: 5205.6x^(-1.22) Number of bands in your unknown protein sample: 3 Distance each band traveled on your gel: A measured at 20 mm B measured at 62 mm C measured at 82 mm What is the subunit composition of this protein? 2 of A, 1 of B, 1 of C 1 of A, 2 of B, 1 of C 1 of A, 1 of B, 2 of C 1 of A, 1 of B, 1 of C
You are working at a major pharmaceutical company, and you have purified an engineered enzyme, and you need to determine the protein stability (kJ/mol). Accordingly, you have collected equilibrium unfolding data using the chemical denaturant urea at 20°C, pH 7.5 and I atmosphere using fluorescence spectroscopy. a) Determine the protein stability (AG [kJ/mol]) via nonlinear least squares (using the available data). b) Write the partial differential equation (i.e., general functional form, variable, constants). c) Describe what would happen to the isotherm if the temperature was increased to 25 °C. Urea [M] 0 0.25 0.5 0.75 1 1.25 1.5 2 2.25 2.5 2.75 3 3.25 3.5 3.75 4 4.25 4.5 4.75 5 FL 340nm 316 315.5 315 314.5 314 315 300 275 225 125 75 60 55 54 53 52.5 52.25 52 51.75 51.5 dG = Vdp-SdT+μA dnд + μB dng dGp = μA dnA+ μg dng A = Folded State B = Unfolded State
The results of a separation using two-dimension gel electrophoresis are shown here. Which protein or proteins have the highest pl value? d and e b and c a Which protein has the highest molecular weight? b d a isoelectric focusing electrophoresis pH 5 a b pH 9 d e SDS PAGE electrophoresis

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