Transport of histidine into a bacterial cell was measured at several different histidine concentrations, see table below. Based onthese data, is histidine uptake facilitated by a carrier or channel protein?abHistidine (uM)2.57163172сSelect an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer.A carrier protein because it becomes saturated.A carrier protein because it does not become saturated.A channel protein because it becomes saturated.Transport (uM/min)dA channel protein because it does not become saturated.42.51192404901000XYour answer

The kinetics of transport of a molecule via a carrier protein and a protein channel differ from each…

Answered: Transport of histidine into a bacterial…

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

Make a table with a scale of absorbance and the concentration of protein in Chromatin sample from the following data for excel graph Absorbance=660nm following data are of tubes with concern A =0 B=0.036 C=0.011 D=0.001 E=0.027 F=0.020 G=0.032 H1=0.176 H2=0.183 I1=0.150 I2=0.171 also plot the graph??
The ACE2 receptor protein in humans has been getting a lot of press these days, as it apparently serves as a "receptor" for the SARS-CoV-2 coronavirus in addition to its normal functions. This protein has an isoelectric pH of 5.36. Suppose you want to purify this protein to study its properties, with the goal of developing a drug that would block it from binding the virus. Once you have purified the cell surface proteins from your cultured human lung cells away from all the other types of molecules in the cell, and all the cytoplasmic proteins, you might decide to use ion exchange chromatography to separate the ACE2 proteins from other proteins in your sample. If you plan to load your protein mixture onto your ion exchange column in a buffer at pH 7.4 (approximately physiological pH) and you want the ACE2 proteins to bind to the column, should you use a resin with a positive charge or a negative charge? Briefly explain why you chose the resin you selected.
Members of the integrin family are the major cell surface receptors for many ECM proteins such as fibronectin. In experimental studies, single integrin heterodimers have been found to assume more than one structural conformation. Describe the relationship between integrin structures and their activities.
For each of the following, describe the path the protein takes to its final destination in the cell.Drawings are strongly recommended! If you need more space, you can use a separate sheet ofpaper. Proteins: 1) Hedgehog (released from the signaling cell), 2) Smoothened, 3) Ci/GliYour answers should include the following if they apply for each protein:o Sorting sequences and how the protein knows where to go at each step (what recognizesdifferent sorting sequences/tags). How/when the protein is inserted into the membrane (if it is a membrane protein) What organelles the protein passes through on its way to its final destination. How the protein is transported (vesicles? translocons? etc.), including a role for microtubules.How the protein might be modified in each organelle it passes through. What other proteins are involved in transport and how the system is reset to allow for otherproteins to be transported.
For each of the following, describe the path the protein takes to its final destination in the cell.Drawings are strongly recommended!Proteins: 1) Hedgehog (released from the signaling cell), 2) Smoothened, 3) Ci/GliYour answers should include the following if they apply for each protein:o Sorting sequences and how the protein knows where to go at each step (what recognizesdifferent sorting sequences/tags)o How/when the protein is inserted into the membrane (if it is a membrane protein)o What organelles the protein passes through on its way to its final destinationo How the protein is transported (vesicles? translocons? etc.), including a role for microtubuleso How the protein might be modified in each organelle it passes througho What other proteins are involved in transport and how the system is reset to allow for otherproteins to be transported
Maintaining nuclear RanGTP levels is critical for nucleo-cytoplasmic transport. Describe how mutations that disrupt RanGEF function would affect the movement of proteins coming in and going out of the nucleus.
Is adenylate cyclase a transmembrane protein or a peripheralprotein? What about the G protein?
A spheroidal bacterium with a diameter of 1.0 mm (micrometer, 1 mm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?
The following observations are made on an unknownmembrane protein, X. It can be extracted from disrupted erythrocyte membranes into aconcentrated salt solution, and it can be cleaved into fragments by proteolytic enzymes. Treatment of erythrocytes with proteolytic enzymes followed by disruption and extraction of membrane components yields intact X. However, treatment of erythrocyte “ghosts” (which consist of just plasma membranes, produced by disrupting the cells and washing outthe hemoglobin) with proteolytic enzymes, followed by disruption and extraction, yields extensively fragmented X. What do these observations indicate about the location of X in the plasma membrane? Do the properties of X resemble those of an integral or peripheral membrane protein?
Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
Human serum transferrin is an iron transport protein. With the use of appropriate diagrams, describe the metal-bound active site and discuss the structural changes that occur on iron binding to the protein.
Consider a transmembrane protein that forms a hydrophilic pore across the plasma membrane of a eukaryotic cell, allowing Na+ to enter the cell when it is activated upon binding a specific ligand on its extracellular side. It is made of five similar transmembrane subunits, each containing a membrane-spanning α helix with hydrophilic amino acid side chains on one surface of the helix and hydrophobic amino acid side chains on the opposite surface. Considering the function of the protein as a channel for Na+ ions to enter the cell, propose a possible arrangement of the five membrane-spanning α helices in the membrane.

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