4) For various amino acid pairs (for example: F to A, E to R, D to N, V to L, S toW), ask yourself:a) Based on what you know about the chemical properties of the side chains,what effect would you expect on the stability of the protein if you mutatedone residue of the pair into the other in the interior of the protein?What forces might have an impact on this change (ie: what types ofinteractions would you expect that amino acid to be involved in?)How would your answer change if the amino acid were located on thesurface of the protein?b)c)

Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…

Answered: 4) For various amino acid pairs (for…

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

Jacqueline isolated an interesting new protein from the broth of a yeast culture. After purification of the protein, she requested an amino acid analysis and found that the protein contained 0.57% tryptophan by weight (tryptophan Mr-204). Calculate the minimum molecular weight of the protein (i.e., assuming there is only one tryptophan residue per protein molecule).
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.
Proline is known as a beta sheet and alpha helix "breaker ," therefore proline is rarely found in beta sheets or alpha helices. why do you think this is? In your explanation, you should describe the specific molecular interactions necessary for the formation of alpha-helices and beta-sheets. Please be as specific as possible.
Using the letter “R" to indicate amino acid side chain, draw the following: A. The backbone atoms and bonds of a parallel ß-sheet with two B-strands of 5 amino acid each (use slide 23 of Chapter 6 for guidance). B. The backbone atoms and bonds of an antiparallel B-sheet with two B-strands of 5 amino acid each (use slide 23 of Chapter 6 for guidance). C. Draw the hydrogen bonds connecting the two B-strands in each B-sheet.
1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensation
16.2
a) Where is the N-terminus of this peptide? Left Middle Right b) What type of secondary structure is the majority of this structure? loops alpha helix Beta sheet unstructured c) The X's indicate the alpha carbons of residues 10, 13, and 17 (labeled in the sequence above). Where would you expect this part of the structure to be found in the tertiary structure of the protein? Briefly explain your reasoning. d) The dashed line in black is indicating an interaction that is present within this structure. Draw this interaction, including all the atoms necessary for this interaction to occur. Label any partial charges present in your drawing. please upload the drawing.
Our understanding of how proteins fold allows us to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence :a)Where might bends or βturns occur? b)Where might intrachain disulphide cross-linkages be formed? c)Assuming that this sequence is part of a bigger globular protein, indicate the probable location (on the surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln and Lys. Explain your reasoning
1. What are the effects of a) amino acid composition and sequence and b) intramolecular and intermolecular forces of attraction to protein folding? 2. What molecular property of amino acids can be used to justity the concept that the "molecular part of the protein can exhibit the same property as the molecular 'whole' (protein molecule?). Provide a comprehensive discussion using one molecular property. 3. Discuss two metabolic disorders which are caused by protein misfolding. Explain the metabolic consequence of the disorder. 4. If a non-science person asks you what protein folding is and how the concept is related to metabolic disorders, how are you going to explain the concept? (please summarize the concepts used, thank you!)
What is the tertiary structure of a protein? What are the main types of tertiary structure?
1) If a mutation caused an alanine to turn in glycine, what kind of effect do you think that would have on the protein structure? Explain your reasoning. 2) If a mutation caused an alanine to turn into a glutamine, what effect do you think that would have on a protein? Explain your reasoning.
Name two(2) interactions that maintain tertiary protein structure.

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