Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro

Marina Ramirez-Alvarado, Melanie J. Cocco, Lynne Regan

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

We previously reported that under certain experimental conditions, many variants of the B1 domain of IgG-binding protein G from Streptococcus form fibrils reproducibly. The variant I6T53 was the focus of the present study because the lag phase in the kinetics of fibril formation by this variant is significantly longer than that of other variants. This lag phase is distinguished by changes in both intrinsic fluorescence intensity and in light scattering of the protein. NMR diffusion measurements suggest that the soluble protein during the lag phase is monomeric. The kinetic profiles of fibril formation are found to depend on experimental conditions. The first kinetic phase diminishes almost completely when the reaction is seeded with preformed amyloid fibrils.

Original languageEnglish (US)
Pages (from-to)567-576
Number of pages10
JournalProtein Science
Volume12
Issue number3
DOIs
StatePublished - Mar 1 2003

Fingerprint

Amyloid
Mutation
Kinetics
Proteins
Light scattering
Fluorescence
Nuclear magnetic resonance
Light
Protein Domains
In Vitro Techniques

Keywords

  • Amyloid
  • Amyloid kinetics
  • Fluorescence
  • Light scattering
  • NMR
  • Protein G B1 domain
  • Sodium sulfate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Mutations in the B1 domain of protein G that delay the onset of amyloid fibril formation in vitro. / Ramirez-Alvarado, Marina; Cocco, Melanie J.; Regan, Lynne.

In: Protein Science, Vol. 12, No. 3, 01.03.2003, p. 567-576.

Research output: Contribution to journalArticle

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