Imagine the main chain of a protein bends back on itself, so that two amino acid residues R₁ and R₂ come close to each other. Here's what R₁ looks like:-CH-CH₂CH₂CH₂CH₂1NH3Could R₁ form a salt bridge with R₂ at physiological pH, if R₂ were the right kind of residue?O yesO noIf you said R₁ could form a sal bridge with R₂, what would R₂ have to be?0If there's only one possibility, write its 3-letter code. If there is more than one possibility, write the3-letter code of any of them.X?BEET号图Ar

Salt bridge is a bond between amino acids which carry opposite charges. The opposite charges exert…

Answered: Imagine the main chain of a protein…

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

1. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 7? 2. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 12?
This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?
8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3
A protein has an asp glu/arg lys ratio of 3. Explain how would the overall charge on this molecule likely be at pH 7 be negative?
Which of the amino acid side-chains would you expect to be protonated (i.e. has not lost its proton) under neutral pH conditions? Include reasons supporting your prediction.
Can you please explain how to solve this problem?
Tertiary structures refer to the three-dimensional arrangement of every atom in the molecule. On the other hand, primary structures refer to the stable arrangements of amino acid residues in a protein that give rise to recurring patterns. O Both statements are correct O Both statements are incorrect O The first statement is incorrect while the second statement is correct O The first statement is correct while the second statement is incorrect
A schematic diagram of the helical structure of cytochrome b562 is reproduced below. Thisprotein belongs to the family of -proteins that have a four-helix bundle. Number the helices 1 – 4according to their N  C direction. Indicate relative orientations of the macrodipoles of helices 1 – 4adjacent to the diagram of cytochrome b562. Remember that according to the definition of a dipolethat the arrow points towards the positive end.
Given below is a sequence of a polypeptide: AVLLRKIFWFDLAG The pKas of different groups/side chains are shown in the table below: Group/side chain pka C-terminus 3.5 Asp 3.9 Glu 4.1 His 6.0 Cys 8.4 Tyr 10.5 Lys 10.5 Arg 12.5 N-terminus 9.0 What is the total charge of this molecule at pH 11? [ Select ] What is the total charge of this molecule at pH 13? [ Select ] What is the isolectric point for this molecule? (Select]
Suppose you have a solution of a protein, which contains a specific Tyr residue that has an actual (measured) pKa of 8.8. The protein binds a ligand by several noncovalent interactions, one of which is a hydrogen bond in which the Tyr phenolic hydroxyl group must serve as a hydrogen bond donor. Calculate the percentage of the protein molecules in which that tyrosyl residue's phenolic hydroxyl group could serve as a hydrogen bond donor at pH 8.5
"Potassium Bromate (KBr03) is added to flour as a softener that strengthens the texture of bread. It can do this by forming disulfide bonds between two cysteine amino acids in a reaction similar to the chemical equation given below. The function of KBr03 is to remove the 2 electrons needed to form the disulfide bond as shown in the figure below. Each of the cysteine amino acids will be in a protein chain, so the reaction binds the two chains together, giving the dough cohesion. However, potassium bromate is a proven carcinogen and is only allowed in foods in the United States because bakers will add the right amount and correct It has been assumed to meet the temperature and cooking time conditions. " KBRO, + C,H¸NO,SH → KBr + H,O+C,H„N,O,S, Balance the reaction of potassium bromate (KBr03) with the cysteine molecule (C3H6 NO2 SH) by converting it into the reduced step matrix using the additive matrix method. (Kis the symbol of potassium in the question) (Homogeneous linear equation…
Create an oligopeptide via dehydration synthesis using the following amino acids. O. H Tryptophan (TRP) C-C-N но сн, C-C-N. но Glycine (GLY) H H HN

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