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Title: Protein Folding Dynamics Detected By Time-Resolved Synchrotron X-ray Small-Angle Scattering Technique

Abstract

The polypeptide collapse is an essential dynamics in protein folding. To understand the mechanism of the collapse, in situ observation of folding by various probes is necessary. The changes in secondary and tertiary structures in the folding process of globular proteins, whose chain lengths are less than 300 polypeptides, were observed by circular dichrosim and intrinsic fluorescence spectroscopies, respectively. On the other hand, those in protein compactness could be only detected by using time-resolved synchrotron x-ray small-angle scattering technique. The observed dynamics for several proteins with different topologies suggested a common folding mechanism termed 'collapse and search' dynamics, in which the polypeptide collapse precedes the formation of the native contact formation. In 'collapse and search' dynamics, the most outstanding feature lied in the compactness of the initial intermediates. The collapsed intermediates demonstrated the scaling relationship between radius of gyration (Rg) and chain length with a scaling exponent of 0.35 {+-} 0.11, which is close to the value (1/3) predicted by mechano-statistical theory for the collapsed globules of polymers in poor solvent. Thus, it was suggested that the initial collapse is caused by the coil-globule transition of polymers. Since the collapse is essential to the folding of larger proteins, further investigationsmore » on the collapse likely lead to an important insight into the protein folding phenomena.« less

Authors:
;  [1];  [2]
  1. RIKEN Harima Institute, SPring-8 Center, Laboratory for Biometal Science, Hyogo 679-5148 (Japan)
  2. (Japan)
Publication Date:
OSTI Identifier:
21056956
Resource Type:
Journal Article
Resource Relation:
Journal Name: AIP Conference Proceedings; Journal Volume: 902; Journal Issue: 1; Conference: 2. international symposium on portable synchrotron light sources and advanced applications, Shiga (Japan), 15-17 Jan 2007; Other Information: DOI: 10.1063/1.2723630; (c) 2007 American Institute of Physics; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; FLUORESCENCE SPECTROSCOPY; MOLECULAR STRUCTURE; POLYMERS; POLYPEPTIDES; PROBES; SMALL ANGLE SCATTERING; SOLVENTS; STATISTICAL MODELS; SYNCHROTRON RADIATION; TIME RESOLUTION; TOPOLOGY; X RADIATION; X-RAY DIFFRACTION

Citation Formats

Fujisawa, Tetsuro, Takahashi, Satoshi, and Institute for Protein Research, Osaka University Suita Osaka 565-0871/CREST, JST. Protein Folding Dynamics Detected By Time-Resolved Synchrotron X-ray Small-Angle Scattering Technique. United States: N. p., 2007. Web. doi:10.1063/1.2723630.
Fujisawa, Tetsuro, Takahashi, Satoshi, & Institute for Protein Research, Osaka University Suita Osaka 565-0871/CREST, JST. Protein Folding Dynamics Detected By Time-Resolved Synchrotron X-ray Small-Angle Scattering Technique. United States. doi:10.1063/1.2723630.
Fujisawa, Tetsuro, Takahashi, Satoshi, and Institute for Protein Research, Osaka University Suita Osaka 565-0871/CREST, JST. Fri . "Protein Folding Dynamics Detected By Time-Resolved Synchrotron X-ray Small-Angle Scattering Technique". United States. doi:10.1063/1.2723630.
@article{osti_21056956,
title = {Protein Folding Dynamics Detected By Time-Resolved Synchrotron X-ray Small-Angle Scattering Technique},
author = {Fujisawa, Tetsuro and Takahashi, Satoshi and Institute for Protein Research, Osaka University Suita Osaka 565-0871/CREST, JST},
abstractNote = {The polypeptide collapse is an essential dynamics in protein folding. To understand the mechanism of the collapse, in situ observation of folding by various probes is necessary. The changes in secondary and tertiary structures in the folding process of globular proteins, whose chain lengths are less than 300 polypeptides, were observed by circular dichrosim and intrinsic fluorescence spectroscopies, respectively. On the other hand, those in protein compactness could be only detected by using time-resolved synchrotron x-ray small-angle scattering technique. The observed dynamics for several proteins with different topologies suggested a common folding mechanism termed 'collapse and search' dynamics, in which the polypeptide collapse precedes the formation of the native contact formation. In 'collapse and search' dynamics, the most outstanding feature lied in the compactness of the initial intermediates. The collapsed intermediates demonstrated the scaling relationship between radius of gyration (Rg) and chain length with a scaling exponent of 0.35 {+-} 0.11, which is close to the value (1/3) predicted by mechano-statistical theory for the collapsed globules of polymers in poor solvent. Thus, it was suggested that the initial collapse is caused by the coil-globule transition of polymers. Since the collapse is essential to the folding of larger proteins, further investigations on the collapse likely lead to an important insight into the protein folding phenomena.},
doi = {10.1063/1.2723630},
journal = {AIP Conference Proceedings},
number = 1,
volume = 902,
place = {United States},
year = {Fri Mar 30 00:00:00 EDT 2007},
month = {Fri Mar 30 00:00:00 EDT 2007}
}