The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are false

The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are false

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,...

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You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.
Structures of proteins comprising domains separated by flexible linker regions can be quite difficult to solve by x-ray crystallographic methods. Why might this be the case? What are possible experimental approaches to circumvent this barrier?
Some proteins migrate anomalously in SDS-PAGE gels. For instance, the molecular weight determined from an SDS-PAGE gel is sometimes very different from the molecular weight determined from the amino acid sequence. Suggest an explanation for this discrepancy.
This SDS-PAGE loading buffer has SDS (a denaturing detergent), β-mercaptoethanol (a reducing agent), Coomassie Blue (a dye), and glycerol. You will need to dilute your protein samples such that the final concentration of the loading buffer is 1x, meaning that you will add 5 parts of the protein sample for every 1 part of 6x buffer. Calculate how much of the 6x loading buffer you will need to add to each sample. Then, add the appropriate amount of 6x SDS-PAGE loading buffer to the samples. Store the samples in the -20°C freezer. What is the final concentration of glycerol in each of the samples?
The major difference between a protein molecule in its native state and inits denatured state lies in the number of conformations available. To a firstapproximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues.(a) For a protein of 100 residues, estimate the entropy change per moleupon denaturation.(b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?(c) Will the fraction denatured increase or decrease with increasingtemperature?
What kind of information is stored in protein three-dimensional structure. Why 3D structure prediction is important? In detail discuss the major factors involved in 3D protein structure prediction and evaluation computationally.
A protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular weight of 200kD. When this protein is run on SDS-PAGE , a sing band is observed at 100kD. Based on these observations, what can be concluded about the structure of the protein? (if applies, choose more than one) The protein consist of two 200kD subiunits The protein has a quaternary structure The protein is madeup of two 100 kD subunits Proteins is a tetramer consisting of 200 kD domains. The protein contains an impurity of 100kD
Peptides and small proteins fold spontaneously in aqueous solution at room temperature. Thus, for a small protein in water, we can say ΔG FOLD < 0. Denoting the unfolded protein as Unf and the folded protein as Fld, we can write the following equation:Unf(aq)--DELTA G FOLD----> Fld(aq)Considering the transition from the unfolded state (in which there are many possible conformations) to the folded state (only one conformation), there is clearly a decrease in the entropy of the protein. However, protein folding is (correctly) described as an entropically driven process.a) Resolve this apparent paradox by identifying the enthalpy (ΔH) and entropy (−TΔS)components involved in protein…
You were asked to separate twoproteins from one another by means of iso-electric focussing. The pI value of proteinA is 4.3 and the pI value of protein B is 6.7. Describe how you would carry out thisanalysis. Use also a schematic outline to illustrate your answe
For backbone assignments of a medium-size protein (~15kD), CBCA(CO)NH and HNCACB experiments need to be run on an NMR sample. Briefly describe the conditions of protein sample labeling and NMR sample. ?
When protein X is subjected to dimethylsuberimidate and SDS electrophoresis a 50 kDa band is seen; when the protein X is subjected to SDS electrophoresis without DMS, two bands of 20 kDa and 10 kDa are seen. How many different oligomeric structures of the native protein X are possible, being consistent with these observed results? one two three none of the above which is the answrr? and explain
A protein with a known mass of 240 kDa is treated with -mercaptoethanol, a sulfhydryl reducing agent. When the resultant peptide mixture was analyzed by SDS PAGE, one protein band of 60 kDa was present. How many disulfide bonds were present in the original structure of the protein? Group of answer choices -4 -2 -1 -3