Studies of protein structure in solution and protein folding using synchrotron small-angle x-ray scattering

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Description

Synchrotron small angle x-ray scattering (SAXS) has been applied to the structural study of several biological systems, including the nitrogenase complex, the heat shock cognate protein (hsc70), and lysozyme folding. The structural information revealed from the SAXS experiments is complementary to information obtained by other physical and biochemical methods, and adds to our knowledge and understanding of these systems.

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188 p.

Creation Information

Chen, Lingling April 1, 1996.

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Description

Synchrotron small angle x-ray scattering (SAXS) has been applied to the structural study of several biological systems, including the nitrogenase complex, the heat shock cognate protein (hsc70), and lysozyme folding. The structural information revealed from the SAXS experiments is complementary to information obtained by other physical and biochemical methods, and adds to our knowledge and understanding of these systems.

Physical Description

188 p.

Notes

OSTI as DE97008275

Source

  • Other Information: TH: Thesis (Ph.D.)

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Identifier

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  • Other: DE97008275
  • Report No.: SLAC-R--498
  • Grant Number: AC03-76SF00515
  • Office of Scientific & Technical Information Report Number: 510600
  • Archival Resource Key: ark:/67531/metadc692131

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Office of Scientific & Technical Information Technical Reports

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Creation Date

  • April 1, 1996

Added to The UNT Digital Library

  • Aug. 14, 2015, 8:43 a.m.

Description Last Updated

  • Aug. 4, 2016, 7:13 p.m.

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Chen, Lingling. Studies of protein structure in solution and protein folding using synchrotron small-angle x-ray scattering, thesis or dissertation, April 1, 1996; Menlo Park, California. (digital.library.unt.edu/ark:/67531/metadc692131/: accessed September 24, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.