Chemistry Chemistry"VDAATFKQANDNG" is the sequence of ana helix. Which of the following interactionsis probable? (. denotes a H-bond)N...AF...VV...AQ...APlease answer it correctly urgently within ahour.You will get 2 upvotes.thanks

VDAATFKQANDNG In alpha-helix : H-bonding occurs b/w ith(CO group) and i+4th(NH group) amino acids.

Answered: "VDAATFKQANDNG" is the sequence of an a…

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) NMR measurements have shown that poly- L -lysine is a random coil at pH 7 but becomes a helix as the pH is raised above 10. Account for this pHdependent conformational transition. (b) Predict the pH dependence of the helix–coil transition of poly- L - glutamate
Below is the primary structure of a protein. A R 1 I I H H || O H 1 Psi bond [Select] Phi bond [Select] N-terminus [Select] B C D H O I || C-terminus [Select] NC-C-N-C-C-N-C-C-N-C-C-N-C-C - N... I 1 H H I R R H I 11 O HO I || R R I I H a. For each part of the question, select the letter associated the with appropriate component of the structure. Peptide bond [Select] I H U MO b. Which letter represents a bond without 360-degree rotation? [Select] H |
Long-range interactions between residues on a single polypeptide chain are classified as quaternary structures. On the other hand, interactions between residues on separate polypeptide chains are classified as tertiary structures. O Both statements are correct O The first statement is correct while the second statement is incorrect O Both statements are incorrect O The first statement is incorrect while the second statement is correct
Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys Cys
rotein which How many: (a) Nitrogenous bases code for the protein? (b) Anticodons code for the protein? (c) Genes code for the protein? Identify the processes labelled 2 and 3. Indicate where process 2 takes place in a cell. Describe the process taking place at 1. Identify molecules A and B respectively. Tabulato TWO
1. Draw the tripeptide: Val-Leu-Met at pH 7 with the N-terminus to the left and C-terminus to the right. On your drawing, do the following: a. Draw a triangle around the alpha carbons. b. Draw a box around the R-groups. c. Circle the atoms capable of hydrogen bonding. d. Highlight the peptide bond. Ma voy bludy 2. What specific atoms in your tripeptide (above) can participate in hydrogen bonding?
A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free –SH group and the other two are involved in an -S-s- bond.
Chicken egg contains a lot of proteins which supports the growth and development of the chicken embryo. The chicken egg was placed on high heat (100°C) until it forms a solid structure. Which of the following statements is correct about the given scenario? O The increase in temperature may interfere intermolecular forces of attraction that stabilizes the native conformation. O Structural and functional characteristics of proteins remain intact even temperature was increased to boiling O Extreme temperature conditions may result to irreversible denaturation due to destruction of primary. secondary, tertiary, and quaternary structures By decreasing the temperature, the egg embryo can still develop, and grow to become a chicken because renaturation may take place.
(a) Draw diagrams to show how the four synthetic oligonucleotides below could base-pair to form a stable model Holliday junction. W 5' GATCGCATTGTAGCCGTAGGTCCACTGTAA 3’ X 5' GTCCCATACGTAGCCGTAGGACATGTACCG 3' Y 5' CGGTACATGTCCTACGGCTACAATGCGATC 3' Z 5' TTACAGTGGACCTACGGCTACGTATGGGAC 3' I and 21
CH3 НО CH3 describe a biochemical function of the structure shown above .......
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.
. Assume that some protein molecule, in its folded native state, has one favored conformation. But, when it is denatured, it becomes a "random coil," with many possible conformations. (a) What must be the sign of AS for the change: native → denatured? (b) How will the contribution of AS for native → denatured affect the favorability of the process? What apparent requirement does this impose on AH if proteins are to be stable structures?

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

"VDAATFKQANDNG" is the sequence of an a helix. Which of the following interactions is probable? (. denotes a H-bond) N...A F...V V...A Q...A