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Formation and Cooperative Behaviour of Protein Complexes on the Cell Membrane (Record no. 26983)

000 -LEADER
fixed length control field 02960nam a22004575i 4500
003 - CONTROL NUMBER IDENTIFIER
control field OSt
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20140310153036.0
007 - PHYSICAL DESCRIPTION FIXED FIELD--GENERAL INFORMATION
fixed length control field cr nn 008mamaa
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 110929s2012 gw | s |||| 0|eng d
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
International Standard Book Number 9783642239885
978-3-642-23988-5
050 #4 - LIBRARY OF CONGRESS CALL NUMBER
Classification number QH601-602
Classification number QR77
082 04 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 571.64
Edition number 23
264 #1 -
-- Berlin, Heidelberg :
-- Springer Berlin Heidelberg,
-- 2012.
912 ## -
-- ZDB-2-PHA
100 1# - MAIN ENTRY--PERSONAL NAME
Personal name Guseva, Ksenia.
Relator term author.
245 10 - IMMEDIATE SOURCE OF ACQUISITION NOTE
Title Formation and Cooperative Behaviour of Protein Complexes on the Cell Membrane
Medium [electronic resource] /
Statement of responsibility, etc by Ksenia Guseva.
300 ## - PHYSICAL DESCRIPTION
Extent XII, 80 p.
Other physical details online resource.
440 1# - SERIES STATEMENT/ADDED ENTRY--TITLE
Title Springer Theses
505 0# - FORMATTED CONTENTS NOTE
Formatted contents note Introduction -- The Role of Fragmentation on the Formation of Homomeric Protein Complexes -- Collective Response of Self-organised Clusters of Mechanosensitive Channels -- Assembly and Fragmentation of Tat Pores -- Conclusion.
520 ## - SUMMARY, ETC.
Summary, etc With the aim of providing a deeper insight into possible mechanisms of biological self-organization, this thesis presents new approaches to describe the process of self-assembly and the impact of spatial organization on the function of membrane proteins, from a statistical physics point of view. It focuses on three important scenarios: the assembly of membrane proteins, the collective response of mechanosensitive channels and the function of the twin arginine translocation (Tat) system. Using methods from equilibrium and non-equilibrium statistical mechanics, general conclusions were drawn that demonstrate the importance of the protein-protein interactions. Namely, in the first part a general aggregation dynamics model is formulated, and used to show that fragmentation crucially affects the efficiency of the self-assembly process of proteins. In the second part, by mapping the membrane-mediated forces into a simplified many-body system, the dynamic and equilibrium behaviour of interacting mechanosensitive channels is derived, showing that protein agglomeration strongly impacts its desired function. The final part develops a model that incorporates both the agglomeration and transport function of the Tat system, thereby providing a comprehensive description of this self-organizing process.
650 #0 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name as entry element Physics.
Topical term or geographic name as entry element Polymers.
Topical term or geographic name as entry element Cell membranes.
Topical term or geographic name as entry element Physics.
Topical term or geographic name as entry element Membranes.
Topical term or geographic name as entry element Membrane Biology.
Topical term or geographic name as entry element Statistical Physics, Dynamical Systems and Complexity.
Topical term or geographic name as entry element Polymer Sciences.
710 2# - ADDED ENTRY--CORPORATE NAME
Corporate name or jurisdiction name as entry element SpringerLink (Online service)
773 0# - HOST ITEM ENTRY
Title Springer eBooks
776 08 - ADDITIONAL PHYSICAL FORM ENTRY
Display text Printed edition:
International Standard Book Number 9783642239878
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier http://dx.doi.org/10.1007/978-3-642-23988-5
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme
Item type E-Book
Copies
Price effective from Permanent location Date last seen Not for loan Date acquired Source of classification or shelving scheme Koha item type Damaged status Lost status Withdrawn status Current location Full call number
2014-04-23AUM Main Library2014-04-23 2014-04-23 E-Book   AUM Main Library571.64

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