=A different Fab fragment binds to lysozyme with a dissociation constant of Ka 10-6 M. A 1 nM (10-9 M) solution oflysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of thelysozyme be bound to this Fab?[F] =abM

Ligand receptor complex is a term used to describe the non-covalent interaction between a ligand and…

Answered: A different Fab fragment binds to…

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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Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?
Which step is catalyzed by the enzyme responsible for the Met 2 mutant? (picture attached) A) homoserine → cysteine B) cysteine → cystathionine C) cystathionine → homocysteine D) homocysteine → methionine E) methionine → homoserine
You have discovered a new hemoglobin variant you are calling Hb-21. You have noticed the following from your studies of Hb-21: - The binding constant of Hb-21 is the same at pH 7.1 and 7.4.- The binding constant curves generated by Hb-21 and O2 are sigmoidal.- The Hill coefficient for Hb-21 is 3.-The binding constant for Hb-21 with O2 in the presence of 5mM 2,3-bisphosphglycerate is about 6-times lower instead of the 8-times lower that is observed under these conditions for the wild type enzyme. Use this information to answer questions: Based on this information which of these features of hemoglobin would you conclude are altered in Hb-21 as compared to the wild type hemoglobin? ____ the cooperativity.____ the amount of T versus R state in the tissues. ____ the Bohr effect. What is the major issue for an individual with the Hb-21 variant? Explain exactly what aspect of hemoglobin’s function is altered.
b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg,Glu,Leu,Lys,Met,Phe,Tyr, Val One fragment from CNBr treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg ii. The reagent shown below is widely utilized in the sequencing of peptides. Treatment of the nonapeptide you deduced in part i. with this reagent yields a phenylthiohydantoin derivative, compound 1, and an octapeptide. Write a mechanism for the formation of compound 1. N=c=8
Imagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbA
In a pUC19 digest for 1 ug of pUC19 (DNA conc. 282ng/ul) using 10X Cutsmart buffer, pure water and BamHI enzyme in a total volume of 40 ul, how much of each solution is added to the total volume?
Please answer the following questions 1) based on the structures of adenine, cytosine, guanine, and thyme. Why does A prefer to bind to T and C prefer to bind to G 2) were the binding energies the same for AT and CG? Explain the difference 3) which of the four know bases is the unknown synthetic base most like in terms of its binding characteristics? What does this indicate about its structure? 4) if the unknown synthetic base was used to study DNA replication, which natural bases would it interact with? 5) is the picture question
Under what conditions will the following partial diploid strain of E. coli convert chorismate to tryptophan (assume trp mutants function similarly to lac mutants)? trpR* trpP trpO* trpE* trpD* trpC* trpB* trpA*/ trpR trpP trpO° trpE trpD trpC trpB trpA ect the one BEST answer (2 oints! O never O only when tryptophan levels are low O constitutively O only when tryptophan is present O only when chorismate levels are low
A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.
Analyse and interpret the SCAM data in Fig. 1, and make a table (remember to include a legend) to indicate where each amino acid is located (cytoplasm, membrane, periplasm).
For each of the following genotypes, explain how mutation (identified by a (-) will affect the organism grown in lactose medium. Indicate whether a) B-galactosidase will be synthesized or not, b) synthesis of B-galactosidase is inducible (1) or constitutive (C) and c) growth of the organism will occur or not. i. I+P+0-Z+Y+A+/l+P+O+Z-Y-A- ii. I-P+0+Z+Y+A+/I+P-O+Z+Y+A+

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A different Fab fragment binds to lysozyme with a dissociation constant of Ka = 10-6 M. A 1 nM (10-9 M) solution of lysozyme is treated with increasing concentrations of this Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to this Fab? [Fab] = M