Detecting in-solution conformational changes in viral fusogens using tryptophan-induced fluorescence quenching

Area of Science:

• Biochemistry
• Structural Biology
• Molecular Biology

Background:

• Dynamic monitoring of protein conformational changes is crucial for understanding biological processes like viral entry.
• Viral glycoproteins undergo significant rearrangements during membrane fusion.

Purpose of the Study:

• To present a protocol for site-specific bimane labeling of influenza-C fusogen.
• To map proximity and conformational movements using tryptophan-induced fluorescence quenching.

Main Methods:

• Site-specific bimane labeling of the influenza-C fusogen.
• Utilizing tryptophan-induced fluorescence quenching to detect proximity and conformational changes.

Main Results:

• The developed protocol enables dynamic monitoring of protein conformational changes.
• The method successfully maps proximity and conformational movements of the viral fusogen.

Conclusions:

• The presented protocol is adaptable for various proteins and protein-protein interaction studies.
• This technique provides insights into the dynamic nature of viral glycoproteins and fusion mechanisms.