MOLECULAR BIOLOGY OF THE CELL (LL)
MOLECULAR BIOLOGY OF THE CELL (LL)
6th Edition
ISBN: 9780393876109
Author: ALBERTS
Publisher: NORTON
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Chapter 14, Problem 10P

A.

Summary Introduction

To explain: Why the actin filaments revolve in steps of ATP synthesis with pause in between and what does the rotation correspond to in terms of the α3β3 γ complex.

Concept introduction:

The total process of ATP synthesis is complex membrane-embedded enzyme that looks like a rounded structure with complete rotation.  The rounded structure of enzyme is regarded as the F1 subunit that protrudes into the mitochondrial matrix and contains the catalytic activity of the enzyme synthase. This subunit contains various polypeptide chains.  The α and β subunit of the polypeptide chain, make up the bulk of the F1 arranged alternatively in the rotational structure. The α and β subunit bind nucleotides but only the β subunits participate directly in catalysis functioning. The γ subunit breaks the symmetric position of the α3β3 hexamer, in each of the β subunits is different by virtue of its interaction with a distinct face of γ.

B.

Summary Introduction

To explain: In this normal mode of operation inside the cell, total how many number of ATP molecules synthesize for each complete 360° rotation of γ subunit.

Concept introduction:

The total process of ATP synthesis is complex membrane-embedded enzyme that looks like a rounded structure with complete rotation.  The rounded structure of enzyme is regarded as the F1 subunit that protrudes into the mitochondrial matrix and contains the catalytic activity of the enzyme synthase. This subunit contains various polypeptide chains.  The α and β subunit of the polypeptide chain, make up the bulk of the F1 arranged alternatively in the rotational structure. The α and β subunit bind nucleotides but only the β subunits participate directly in catalysis functioning. The γ subunit breaks the symmetric position of the α3β3 hexamer, in each of the β subunits is different by virtue of its interaction with a distinct face of γ.

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