4 edition of Membrane dynamics and domains found in the catalog.
Membrane dynamics and domains
Published
2004
by Kluwer Academic/Plenum in Dordrecht, London
.
Written in English
Edition Notes
Includes bibliographical references and index.
Statement | edited by Peter J. Quinn. |
Series | Subcellular biochemistry -- v. 37. |
Contributions | Quinn, P. J. |
Classifications | |
---|---|
LC Classifications | QH611 S84 37 |
The Physical Object | |
Pagination | xvi, 499 p. : |
Number of Pages | 499 |
ID Numbers | |
Open Library | OL18215489M |
ISBN 10 | 0306484250 |
Cellular Transport and Membrane Dynamics of the Glycine membrane domains, in rat cerebellar. granule cells developing in vitro. J. Biol. Chem. , – dynamics of the domains presumably facilitating their delivery to BAM for folding into the outer membrane. Results. Inter-domain conformational flexibility in SurA We first investigatedthe structure and dynamics of apo-SurA in solutionusing XL-MS, which provides distance information in the form of spatial restraints, and enables comparison of the.
ABUNDANT OIL BODIES IN SEED CELLS: DYNAMIC FUNCTIONS OF MEMBRANE PROTEINS. Oil body formation begins on the endoplasmic reticulum (ER) membrane (Fig. 2A; Chapman et al., ).Storage lipids are produced by lipid biosynthetic enzymes on the ER and then stored in the space between two leaflets of the ER phospholipid bilayer (Yen et al., ).Oil bodies bud off from Cited by: The extraction would take advantage of lipid raft resistance to non-ionic detergents, such as Triton X or Brij at low temperatures (e.g., 4 °C). When such a detergent is added to cells, the fluid membrane will dissolve while the lipid rafts may remain intact and could be extracted. [citation needed].
The BAR domain protein family plays a key role in the formation and detection of local membrane curvatures and in attracting other proteins, including the regulators of actin dynamics. Membrane Binding of C1 Domains. Structural and mutation studies of PKCδ-C1B have defined the phorbol ester/DAG binding polar binding pocket is located at the tip of the molecule and is surrounded by aliphatic and aromatic residues, which are adjoined by a ring of cationic residues in the middle part of the molecule (Fig. 2).
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The fluid-mosaic model of membrane structure formulated by Singer and Nicolson in the early s has proven to be a durable concept in terms of the principles governing the organization of the Format: Hardcover.
The fluid-mosaic model of membrane structure formulated by Singer and Nicolson in the early s has proven to be a durable concept in terms of the principles governing the organization of the constituent lipids and proteins. About this book. Introduction. The fluid-mosaic model of membrane structure formulated by Singer and Nicolson in the early s has proven to be a durable concept in terms of the principles governing the organization of the constituent lipids and proteins.
During the past 30 or so years a great deal of information has accumulated on the composition of various cell membranes and how this is related to the dif ferent functions that membranes. Membrane proteins that have a single anchor near their COOH-terminus require a stop-transfer sequence to form a permanent transmembrane segment and, finally, cleavage of the initial signal peptide.
Many membrane proteins contain two or more topogenic sequences. An example is opsin, which traverses the membrane seven times (Chap. 47). The fluid-mosaic model of membrane structure formulated by Singer and Nicolson in the early s has proven to be a durable concept in terms of the principles governing the organization of the constituent lipids and proteins.
During the past 30 or so years a great deal of information has accumulated on the composition of various cell membranes and how this is related to the dif ferent.
Knowledge about details of these highly dynamic processes rapidly increased in recent years, the book therefore provides a timely summary on the processes of calcium signaling and related membrane dynamics; it is aimed at students and researchers in biochemistry and cell biology.
The lipid composition is consistent with formation of liquid-ordered phases. The present evidence favours a model in which the lateral segregation of membrane proteins takes place on the basis of their affinity for liquid-ordered lipid domains within the by: 8.
Dynamic lipid-protein interactions on the cell membrane influences the distribution of these molecular components in the bilayer and results in the formation of distinct membrane domains, such as lipid rafts.
Such membrane domains serve as precursor sites for the formation of vesicles, invaginations, and protrusions that are essential for the. The combination of a high density of integral membrane proteins with bulky extra-bilayer domains, and of peripheral proteins interacting with both lipids and integral protein polar domains leads to a situation in which the lateral diffusion of proteins is severely restricted, something that Singer and Nicolson could not envisage in Cited by: Lipid phase formation in model membranes.
Studies on model membranes composed of specific lipid mixtures have brought to light some important features of domain formation and their implications at cell membrane level (London, ).Differential interactions between components are the main driving force responsible for the segregation of components into by: Membrane Dynamics and Signaling (Fundamentals of Medical Cell Biology) by E.
Edward Bittar (Editor) ISBN ISBN Why is ISBN important. ISBN. This bar-code number lets you verify that you're getting exactly the right version or edition of a book. Membrane dynamics and domains. [Peter J Quinn;] -- This volume assembles contemporary evidence of domain formation in membranes gathered by leading researchers in fields ranging from membrane biophysics to cell biology.
How to Cite. Tamm, L. K., Kiessling, V. and Wagner, M. Membrane Dynamics. eLS. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but its mechanisms of client binding and chaperone function have remained unclear.
Membrane Dynamics and Domains by Peter J. Quinn,available at Book Depository with free delivery worldwide. This chapter focuses on the nature and function of these two-dimensional membrane domains and highlights several examples of microbial exploitation of host cell membrane organization.
Cholesterol is an important component of most membranes of mammalian cells, and disruption of its homeostasis or distribution in intracellular membranes leads to debilitating disease in : Lynda M. Pierini, Frederick R. Maxfield. The fluid-mosaic model of membrane structure formulated by Singer and Nicolson in the early s has proven to be a durable concept in terms of the principles.
The Membranes of Cells, Third Edition, provides a basic guide to biomembranes, connecting researchers to the numerous fields of biology. The new edition offers a complete update of content based on new understandings in the field.
Foundational content for graduate students, researchers, professors, and undergraduate students across the sciences is provided, succinctly covering all of the basic. 12 determinant for their localization to membrane domains, since deacylated versions of some 13 REMs 4, 17remain able to localize to membrane domains.
The specificity of targeting, the 14 anchoring and nanoclustering mechanisms mediated by REM-CA to the PM inner-leaflet 15 nanodomains remain therefore elusive. Book Description. Cell Membrane Nanodomains: From Biochemistry to Nanoscopy describes recent advances in our understanding of membrane organization, with a particular focus on the cutting-edge imaging techniques that are making these new discoveries possible.
With contributions from pioneers in the field, the book explores areas where the application of these novel techniques reveals new. The C-terminus of most I-BAR domain proteins contains an actin monomer binding WASP-homology 2 (WH2) domain, suggesting that they function at the interface of plasma membrane and actin dynamics.
Additionally, an SH3 domain is present in IRSp53, IRTKS, and FLJCited by: The periplasmic chaperone SurA plays a key role in outer membrane protein (OMP) biogenesis. E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but how it binds its OMP clients and the mechanism(s) of its chaperone action remain unclear.
Here, we have used chemical cross-linking, hydrogen-deuterium exchange, single-molecule FRET and molecular dynamics Author: Antonio N Calabrese, Bob Schiffrin, Matthew A Watson, Theodoros K Karamanos, Martin Walko, Julia R H.We discuss the principles of partitioning of proteins into membranes and how the structure, dynamics, and function of membrane-embedded and peripheral proteins can be modulated by specific membrane components and physical properties of membranes and raft domains.
Finally, we discuss challenges and future directions toward Cited by: