what are the steps to the answer? If a particular 180 amino acid polypeptide is known to sample 3 preferred states as it folds into its native protein conformation, and if10¹4 conformations can be sampled per second, then how many hours would it take for this protein to fold according to Leventhal?6 x 10718 x 1010706 x 10¹707 × 10⁹⁰04 x 1023

Anfinsen's experiment showed that the protein is intrinsically capable of finding its lowest-energy…

Answered: If a particular 180 amino acid…

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

See similar textbooks

Similar questions

A hypothetical protein has a molar mass of 23,300 Da. Assume that the average molar mass of an amino acid is 120. • How many amino acids are present in this hypothetical protein? • What is the minimum number of codons present in the mRNA that codes for this protein? • What is the minimum number of nucleotides needed to code for this protein?
An enzyme consists of 1 polypeptide chain only and has a molecule weight of 30,000. Assuming the average wt. of an amino acid is 100, how many nucleotides are there in the gene controlling it?
You are given a protein solution with a concentration of 0.15 mg/ml. Suppose that we want to prepare a solution containing 100 μg of the protein at a concentration of 1 mg/ml. To achieve this, we will first dry down enough protein solution to obtain 100 μg of proteins. How much solution do we need for drying down? How much volume of H2O do we need to add to the dried protein to obtain the desired concentration?
Assume you were given a mixture consisting of one molecule each of all possible sequences of a smallish protein of molecular weight 4800 daltons. If the average molecular weight of an amino acid is, say, 120 daltons, how much would the sample weigh? How big a container would you need to hold it?
What is the approximate molecular weight of a protein with 682 amino acid residues in a single polypeptide chain?
Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why not
A protein sample of unknown concentration was placed in a cuvette with a path length of 1 cm and the sample was found to have an A280 value of 2.92. If the protein of interest has an extinction coefficient of 44240 M-1 cm-1 and the molecular weight of the protein is 47.411 kDa, what is the concentration of protein in mg/mL?
For each of the following denaturing agents, explain the changes that you observed when each of them is added to an egg white in terms of change in protein structure at the molecular level. 1. heat 2. salt 3. baking soda 4. lemon juice 5. ethyl alcohol
What is the molecular basis for the observation that the overall charge on a protein becomes increasingly positive as pH drops and more negative as pH increases?
Considering the chemical characteristics of the amino acids valine and glutamic acid (see Figure 5.14), propose a possible explanation for the dramatic effect on protein function that occurs when valine is substituted for glutamic acid.
Why do the pK values of ionizable groups differ between free amino acids and amino acid residues in polypeptides?
In kilodaltons (KDa), what is the predicted molecular mass of the protein encoded by this gene CAGATTGTGAAGAGGTCTCTTGA? Answer in numerical digits only

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS