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Polymer chain dynamics in solution probed with a fluorescence blob model

Article Abstract:

The new fluorescence tool coined the fluorescence blob model (FBM) that characterizes the chain dynamics of polymers in solution and is employed to analyze the fluorescence decays of polymers randomly labeled with pyrene, is described. The FBM provides information about polymer chain dynamics by establishing a relationship between number of monomers making up a blob, and the lifetime of pyrene used as an internal clock.

Author: Duhamel, Jean
Publisher: American Chemical Society
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
Polymers, Spectra, Fluorescence spectroscopy, Structure, Chain reactions

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Elucidation of residue-level structure and dynamics of polypeptides via isotope-edited infrared spectroscopy

Article Abstract:

Infrared spectroscopy is a powerful tool for analyzing the structure of proteins and peptides. Site-specific structural information can be obtained by sequential, systematic labeling of the backbone and this method of isotope-edited infrared spectroscopy is a tool for obtaining medium-resolution information about the backbone conformation and dynamics.

Author: Decatur, Sean M.
Publisher: American Chemical Society
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
Massachusetts, Polypeptides, Infrared spectroscopy

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Solid-state NMR studies of the structure, dynamics, and assembly of beta-sheet membrane peptides and alpha-helical membrane proteins with antibiotic activities

Article Abstract:

The NMR methods used to determine the conformation, orientation, depth of insertion, oligomerization, mobility and lipid interaction of membrane peptides and proteins are reviewed. These studies highlight how the peptides disrupt lipid membrane and provide fundamental insights into the folding of beta-sheet and alpha-helical membrane proteins.

Author: Hong, Mei
Publisher: American Chemical Society
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
Iowa, Membrane proteins, Nuclear magnetic resonance

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Subjects list: Analysis, Optical properties, Chemical properties
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