Membrane proteins : folding, association, and design / edited by Giovanna Ghirlanda, Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ, USA, Alessandro Senes, Department of Biochemistry, University of Wisconsin-Madison, Madison, WI, USA.

Contributor(s): Ghirlanda, Giovanna [editor.] | Senes, Alessandro [editor.]
Material type: TextTextSeries: Methods in molecular biology (Clifton, N.J.): v. 1063.Publisher: [Totowa, New Jersey] : Humana Press, [2013]Copyright date: ©2013Description: 1 online resource (x, 246 pages) : illustrations (some color)Content type: text Media type: computer Carrier type: online resourceISBN: 9781627035835; 1627035834; 1627035826; 9781627035828Subject(s): Membrane proteins | Biochemical Phenomena | Membranes, Artificial | Proteins | Biophysical Phenomena | Membrane Lipids | Genetic Engineering | Genetic Techniques | Lipids | Biomimetic Materials | Amino Acids, Peptides, and Proteins | Chemical Phenomena | Physical Phenomena | Manufactured Materials | Chemicals and Drugs | Investigative Techniques | Technology, Industry, and Agriculture | Phenomena and Processes | Analytical, Diagnostic and Therapeutic Techniques and Equipment | Technology, Industry, Agriculture | Membrane Proteins | Protein Folding | Lipid Bilayers | Protein Engineering | Human Anatomy & Physiology | Health & Biological Sciences | Animal Biochemistry | Membrane proteins | membranen | membranes | eiwitten | proteins | Proteins and Enzymes | Eiwitten en enzymenGenre/Form: Electronic books. Additional physical formats: Print version:: Membrane proteins.DDC classification: 572/.696 LOC classification: QP552.M44 | M46 2013Online resources: Click here to access online
Contents:
Use of Thiol-Disulfide Exchange Method to Study Transmembrane Peptide Association in Membrane Environments -- Measurement of Transmembrane Peptide Interactions in Liposomes Using Fr ster Resonance Energy Transfer (FRET) -- Measuring Transmembrane Helix Interaction Strengths in Lipid Bilayers Using Steric Trapping -- Genetics Systems for Monitoring Interactions of Transmembrane Domains in Bacterial Membranes -- Analyzing the Effects of Hydrophobic Mismatch on Transmembrane -Helices Using Tryptophan Fluorescence Spectroscopy -- Folding Alpha Helical Membrane Proteins into Liposomes In Vitro and Determination of Secondary Structure -- Solvation Models and Computational Prediction of Orientations of Peptides and Proteins in Membranes -- Membrane Protein Structure Determination: Back to the Membrane -- On the Role of NMR Spectroscopy for Characterization of Antimicrobial Peptides -- Prediction and Design of Outer Membrane Protein-Protein Interactions -- Design of Transmembrane Peptides: Coping with Sticky Situations -- Engineering and Utilization of Reporter Cell Lines for Cell-Based Assays of Transmembrane Receptors -- Fluorination in the Design of Membrane Protein Assemblies.
Summary: Focusing on model systems for the study of structure, folding, and association in the membrane, Membrane Proteins: Folding, Association, and Design presents an overview of methods that can be applied to these intricate systems. The volume is divided into four detailed sections, covering association of transmembrane helices, interactions with the lipid bilayer, NMR methods, as well as a variety of engineering approaches. Written for the highly successful Methods in Molecular Biology series, 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 practical, Membrane Proteins: Folding, Association, and Design serves as an ideal guide for researchers reaching for the tantalizing possibility of designing novel membrane proteins with tailored functionality.
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Online resource; title from PDF title page (SpringerLink, viewed October 10, 2013).

Use of Thiol-Disulfide Exchange Method to Study Transmembrane Peptide Association in Membrane Environments -- Measurement of Transmembrane Peptide Interactions in Liposomes Using Fr ster Resonance Energy Transfer (FRET) -- Measuring Transmembrane Helix Interaction Strengths in Lipid Bilayers Using Steric Trapping -- Genetics Systems for Monitoring Interactions of Transmembrane Domains in Bacterial Membranes -- Analyzing the Effects of Hydrophobic Mismatch on Transmembrane -Helices Using Tryptophan Fluorescence Spectroscopy -- Folding Alpha Helical Membrane Proteins into Liposomes In Vitro and Determination of Secondary Structure -- Solvation Models and Computational Prediction of Orientations of Peptides and Proteins in Membranes -- Membrane Protein Structure Determination: Back to the Membrane -- On the Role of NMR Spectroscopy for Characterization of Antimicrobial Peptides -- Prediction and Design of Outer Membrane Protein-Protein Interactions -- Design of Transmembrane Peptides: Coping with Sticky Situations -- Engineering and Utilization of Reporter Cell Lines for Cell-Based Assays of Transmembrane Receptors -- Fluorination in the Design of Membrane Protein Assemblies.

Includes bibliographical references and index.

Focusing on model systems for the study of structure, folding, and association in the membrane, Membrane Proteins: Folding, Association, and Design presents an overview of methods that can be applied to these intricate systems. The volume is divided into four detailed sections, covering association of transmembrane helices, interactions with the lipid bilayer, NMR methods, as well as a variety of engineering approaches. Written for the highly successful Methods in Molecular Biology series, 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 practical, Membrane Proteins: Folding, Association, and Design serves as an ideal guide for researchers reaching for the tantalizing possibility of designing novel membrane proteins with tailored functionality.

English.

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