QUESTION 4Approximately how many domains are in an 82.5 kDa protein?O a. 2O b.3"C. 4d. 1QUESTION 5How long is an a-helix that contains 36 amino acid residues?6.0 nm5.4 nm1.8 nm4.8 nmQUESTION 6entropy gain in ES formation.O TrueO False

Domains are the regions of protein primary structure that vary in length from 50 aminoacids to 250…

Answered: Approximately how many domains are in…

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

Green Fluorescent Protein has regions that are very hydrophobic. What is the meaning of “hydrophobic”? What causes a protein to be hydrophobic?
Match the following: At what level of protein structure do B-sheets of amino acids and a-helices, located at a distance from each other along the length of a polypeptide chain, come together to form a globular protein? 6. 12 This protein structure is the result of two or more protein sub-units assembling to form a larger, biologically active protein complex. 15 1. primary structure -- 2. secondary structure 18 What level of protein structure describes amino acid sequence such as Gly- Ala-Val-Ser-Glu-Glu-Tyr- His? 3. tertiary structure 21 4. quaternary structure 24 At what level of protein structure do the chains of amino acids fold into an a- helical structure?
Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3.
Helicases are motor proteins that translocate on nucleic acids: Describe the structure of the conserved RecA fold of helicases
The enzyme thermolysin cleaves peptide bonds on the C-terminal side of the amino acids lle, Tyr, Phe, and Trp. If thermolysin acts on the sequence below: QRYKKSHTWDPNRKLFNRYLCMA which of the figures below shows the structure of the N-terminal residue of the longest fragment? NH3 HO, NH2 HOʻ NH3 NH `NH3 CH3 0 H3C° NH3
A typical animal cell is thought to contain some 10 billion protein molecules that need to be sorted into their proper compartments. That’s a lot of proteins! Can 10 billion proteins even fit into a cell? The average length of a human protein is 450 amino acids, and the average mass of an amino acid in a protein is 110 daltons (1 dalton = 1 g/mol). Given that the average density of a protein is 1.4 g/cm3, what fraction of the volume of a cell would 10 billion average protein molecules occupy? Consider first a liver cell, which has a volume of about 5000 µm3. Then consider a pancreatic β cell, which has a volume of 1000 µm3.
The drop-down answers choices for questions 1 through 4 are NH3, COOH, CH2, or OH. The drop-down answers choices for questions 5 through 6 are negative, neutral but polar, neutral and hydrophobic, or positive. The drop-down answer choices for question 7 is a picture attached below.
Chemistry explain how the change is chemical character that occurs with the missense mutation will influence the tertiary or quaternary structure of the protein (FGFR3). How will the change in shape cause LOF or GOF. be specific! amino acid in missense mutation= S249C serine: polar uncharged, phosphorylated cysteine: nonpolar or polar, disulfide bond
I-D-E-L-Y-S-Q-V-C-S-H-L-D-T-V-R This amino acid sequence forms an alpha helix. What side would face the solvent and what side would face the inside of the protein when thinking of the tertiary structure?
Make a comparison between the teasons for the different flexibility that proteins that consists mainly of a beta sheet structure compared to proteins that consist mainy of alpha helices.
2 / 9 100% +| 1. Explain why only small areas of the Ramachandran plot (below) are occupied (shaded grey) and what the two dark grey shaded areas represent in terms of a protein structure. +180 120 60 -60 -120 -180 -180 -120 -60 60 120 +180
in what groups can we subdivide the amino acids pick one or more A. Amino acids with polar side chains B. amino acids with acidic electrically charged side chains C. amino acid with amphipathic charge side chains D. amino acids with nonpolar side chains E.amino acids with basic electrically charged side chains What is the process of polymerization in proteins? Pick one A. Amino acids are added to a polypeptide strand B. nucleic acids are added to a polypeptide strand C. amino acids are removed from a polypeptide strand D. the cross-linking of different polypeptide strands

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

Approximately how many domains are in an 82.5 kDa protein? O a. 2 Ob.3 OC 4 O d.1 QUESTION 5 How long is an a-helix that contains 36 amino acid residues? 6.0 nm 5.4 nm 1.8 nm 4.8 nm