Achieving Secondary Structural Resolution in Kinetic Measurements of Protein Folding: A Case Study of the Folding Mechanism of Trp‐cage

Cage Folding (DSP implementation) Helix (gastropod)
DOI: 10.1002/ange.201104085 Publication Date: 2011-09-29T08:31:55Z
ABSTRACT
Eine überraschende Wendung: neuartige Multisonden- und Multifrequenzmethode ermöglicht die Untersuchung der Faltungsdynamik individueller Proteinstrukturelemente. Ausgelöst durch einen Temperatursprung entfaltet sich 310-Helix (blau im Bild) des Miniproteins Trp-cage vor globalen Entfaltung Proteins, während Bildung Käfigstruktur von Faltung α-Helix (rot) abhängt. Detailed facts of importance to specialist readers are published as "Supporting Information". Such documents peer-reviewed, but not copy-edited or typeset. They made available submitted by the authors. Please note: The publisher is responsible for content functionality any supporting information supplied Any queries (other than missing content) should be directed corresponding author article.
SUPPLEMENTAL MATERIAL
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