Protein folding dynamics detected by time-resolved synchrotron X-ray small-angle scattering technique

Tetsuro Fujisawa, Satoshi Takahashi

Research output: Chapter in Book/Report/Conference proceedingConference contribution

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 (R g ) 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.

Original languageEnglish
Title of host publicationPORTABLE SYNCHROTRON LIGHT SOURCES AND ADVANCED APPLICATIONS
Subtitle of host publication2nd International Symposium on Portable Synchrotron Light Sources and Advanced Applications
Pages89-92
Number of pages4
DOIs
Publication statusPublished - 2007 May 11
Externally publishedYes
Event2nd International Symposium on Portable Synchrotron Light Sources and Advanced Applications - Shiga, Japan
Duration: 2007 Jan 152007 Jan 17

Publication series

NameAIP Conference Proceedings
Volume902
ISSN (Print)0094-243X
ISSN (Electronic)1551-7616

Conference

Conference2nd International Symposium on Portable Synchrotron Light Sources and Advanced Applications
CountryJapan
CityShiga
Period07/1/1507/1/17

Keywords

  • Coil-globule transition
  • Protein folding

ASJC Scopus subject areas

  • Physics and Astronomy(all)

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  • Cite this

    Fujisawa, T., & Takahashi, S. (2007). Protein folding dynamics detected by time-resolved synchrotron X-ray small-angle scattering technique. In PORTABLE SYNCHROTRON LIGHT SOURCES AND ADVANCED APPLICATIONS: 2nd International Symposium on Portable Synchrotron Light Sources and Advanced Applications (pp. 89-92). (AIP Conference Proceedings; Vol. 902). https://doi.org/10.1063/1.2723630