SaplingPlus for Lehninger Principles of Biochemistry (Six-Month Access)
SaplingPlus for Lehninger Principles of Biochemistry (Six-Month Access)
7th Edition
ISBN: 9781319108236
Author: David L. Nelson, Michael M. Cox
Publisher: W. H. Freeman
bartleby

Videos

Question
Book Icon
Chapter 12, Problem 11P
Summary Introduction

To compare: The G protein-Gs that acts in transducing signal from β-adrenergic receptors and G protein Ras

Introduction: G protein is named due to their binding activity with guanine nucleotide such as GDP and GTP. They are made of three different subunits and are called heterotrimers which is associated with inner surface of plasma membrane and G protein-coupled receptors.

Summary Introduction

To explain: The properties shared by G proteins-Gs and Ras protein.

Introduction: The G proteins are made of three different subunits and are called heterotrimers which is associated with inner surface of plasma membrane and G protein-coupled receptors. It is named so due to their binding activity with guanine nucleotide such as GDP and GTP.

Summary Introduction

To explain: The difference between Gs protein and Ras protein.

Introduction: G protein consists of three subunits such as Gα, Gβ and Gγ. Gα carries a binding site for nucleotide. Gβ and Gγ are associated with inner surface of plasma membrane and G protein-coupled receptors. They are named as G protein due to their binding with guanine nucleotide such as GDP and GTP.

Summary Introduction

To determine: The functional difference between Gs and Gi.

Introduction: G protein is named due to their binding activity with guanine nucleotide such as GDP and GTP. They are made of three different subunits and are called heterotrimers which is associated with inner surface of plasma membrane and G protein-coupled receptors.

Blurred answer
Students have asked these similar questions
For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s. a) Calculate the Ks and KM for this reaction. b) Does substrate binding achieve equilibrium or steady state?
Assume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?
An enzyme lowers the activation energy, (AG) of a reaction from 50.0 kcal/mol to 40.0 kcal/mol. Calulate the catalytic power at 310K. (R-1.987x10 kcal/mol)
Knowledge Booster
Background pattern image
Biochemistry
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.
Similar questions
SEE MORE QUESTIONS
Recommended textbooks for you
Text book image
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Text book image
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Text book image
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
What is Metabolism?; Author: Stated Clearly;https://www.youtube.com/watch?v=nRq6N5NGD1U;License: Standard youtube license