Mechanisms of Outer Membrane Protein Folding PDF Download
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Author: Lindsay Madeline McMorran
Publisher:
ISBN:
Category :
Languages : en
Pages : 520
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Book Description
Author: Lindsay Madeline McMorran
Publisher:
ISBN:
Category :
Languages : en
Pages : 520
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Book Description
Author: Bruce Alberts
Publisher:
ISBN: 9780815332183
Category : Cytology
Languages : en
Pages : 0
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Book Description
Author: Susan Buchanan
Publisher: Humana
ISBN: 9781493928705
Category : Science
Languages : en
Pages : 0
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Book Description
This volume is comprised of a collection of experimental protocols for common techniques and strategies used to study the biogenesis of b-barrel outer membrane proteins in Gram-negative bacteria. The BAM Complex: Methods and Protocols guides readers through methods on the function of the BAM complex, the roles played by each of the individual components, the expression and purification of the components, crystallization and structure determination of the components, and how the individual Bam components may assemble into a functional complex. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and cutting-edge, The BAM Complex: Methods and Protocols will serve as an invaluable reference for those interested in studying the BAM complex.
Author: Gerard Herman Marleen Huysmans
Publisher:
ISBN:
Category :
Languages : en
Pages : 372
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Book Description
Author: Guipeun Kang
Publisher:
ISBN: 9781321852677
Category :
Languages : en
Pages : 179
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Book Description
Approximately 30 % of human genes encode for membrane proteins. Membrane proteins play important roles in cells as ion pumps, ligand receptors, and ion channels, and are targets for approximately 60 % of all therapeutic drugs. Despite their relevance in biology and biochemistry, membrane proteins account for only 1 % of the total number of reported protein structures (RCSB Protein Data Bank), and only 16 % of all protein folding literature is related to membrane protein folding (literature search from 1990 -- 2015, Web of Science). This dissertation presents spectroscopic studies of the in vitro folding mechanisms of outer membrane protein A (OmpA). Several optical tools are utilized, including circular dichroism (CD), tryptophan fluorescence, Förster resonance energy transfer (FRET), and ultraviolet resonance Raman (UVRR) spectroscopy. An improved method to determine free energies of unfolding of OmpA based on spectral decomposition is presented. Dynamics of OmpA folding in synthetic lipid bilayers of small unilamellar vesicles (SUVs) are investigated through studies of secondary and tertiary structures. CD and FRET data indicate that secondary and tertiary structures are formed within the first hour of folding, and strand extension and equilibration continues on a longer timescale. UVRR data complement the CD and FRET results, and reveal evolution of molecular interactions during folding. In particular, a tryptophan residue in the extra-vesicle portion of the pore (position 129) displays unusually intense Raman activity in the hydrogen-out-of-plane (HOOP) region. The increase in HOOP intensity is hypothesized to reflect perturbation of the indole ring electron density because of a nearby charged residue or hydroxyl group on neighboring threonine residue. More likely, hydrogen bonding of [pi] electrons on tryptophan with hydroxyl group contributes to the overall stability in addition to hydrophobic contacts by neighboring hydrophobic residues. A relatively new folding environment of nanodiscs is also explored. Preliminary FRET and UVRR data show that OmpA folds and inserts into nanodiscs. Collectively, these measurements elucidate changes in secondary and tertiary structures as well as molecular interactions of tryptophan residues during membrane protein folding.
Author: Gunnar von Heijne
Publisher: R. G. Landes
ISBN:
Category : Science
Languages : en
Pages : 300
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Book Description
Author: Jos A.F. Op den Kamp
Publisher: Springer Science & Business Media
ISBN: 3642731848
Category : Science
Languages : en
Pages : 474
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Book Description
Many individual aspects of the dynamics and assembly of biological membranes have been studied in great detail. Cell biological approaches, advanced genetics, biophysics and biochemistry have greatly contributed to an increase in our knowledge in this field.lt is obvious however, that the three major membrane constituents - lipids, proteins and carbohydrates- are studied, in most cases separately and that a coherent overview of the various aspects of membrane biogenesis is not readily available. The NATO Advanced Study Institute on "New Perspectives in the Dynamics of Assembly of Biomembranes" intended to provide such an overview: it was set up to teach students and specialists the achievements obtained in the various research areas and to try and integrate the numerous aspects of membrane assembly into a coherent framework. The articles in here reflect this. Statting with detailed contributions on phospholipid structure, dynamics, organization and biogenesis, an up to date overview of the basic, lipidic backbone of biomembranes is given. Extensive progress is made in the research on membrane protein biosynthesis. In particular the post- and co-translational modification processes of proteins, the mechanisms of protein translocation and the sorting mechanisms which are necessary to direct proteins to their final, intra - or extracellular destination have been characterized in detail. Modern genetic approaches were indispensable in this research area: gene cloning, hybrid protein construction, site directed mutagenesis and sequencing techniques elucidated many functional aspects of specific nucleic acid and amino acid sequences.
Author: Charles Tanford
Publisher:
ISBN:
Category : Science
Languages : en
Pages : 256
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Book Description
This almost entirely rewritten edition remains the only comprehensive, up-to-date account of the subject available today—with nearly half of all literature references made to work done since 1973. Theoretical treatment of micelle formation has been greatly improved, making it possible to predict (from first principles) the size and size distribution of micelles formed by many simple amphiphiles . . . as well as the critical concentration at which they first form. Defines four distinct modes of association between protein and detergents (or other amphiphiles), and gives a plausible explanation to show why some ionic detergents generally denature proteins while nonionic detergents often do not. Also includes entirely new chapters on serum lipoproteins and on membrane proteins.
Author: Roger H. Pain
Publisher: Oxford University Press, USA
ISBN:
Category : Medical
Languages : en
Pages : 486
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Book Description
The process by which newly synthesized polypeptide chains become their final 3-dimensional protein forms is clearly explained, providing students and researchers of various backgrounds with both a conceptual and technical understanding of the subject. The new Second Edition incorporates the significant improvements in the field such as advances in interpreting observed kinetic data, the development of technology to observe fast folding reactions, the molten globule state, and the vital role of chaperone proteins in protein folding. The emphasis on experimental approaches has been maintained but this edition does so within the explicit context of simulations and energy surfaces. New discoveries of the central importance of protein folding and unfolding reactions in biology and medicine (including mutation and 'misfolding') are carefully explored. Three case studies elucidate the difficulties of studying protein folding in vivo.
Author: Carmen Domene
Publisher: Royal Society of Chemistry
ISBN: 1782626697
Category : Science
Languages : en
Pages : 275
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Book Description
Exploring current themes in modern computational and membrane protein biophysics, this book presents a comprehensive account of the fundamental principles underlying different methods and techniques used to describe the intriguing mechanisms by which membrane proteins function. The book discusses the experimental approaches employed to study these proteins, with chapters reviewing recent crucial structural advances that have allowed computational biophysicists to discern how these molecular machines work. The book then explores what computational methods are available to researchers and what these have taught us about three key families of membrane proteins: ion channels, transporters and receptors. The book is ideal for researchers in computational chemistry and computational biophysics.
