Although fluorine plays only a minor role in biology, its physicochemical properties have
proven incredibly useful in the design of analogues of biologically important molecules …

Proteins provide much of the scaffolding for life, as well as undertaking a variety of essential
catalytic reactions. These characteristic functions have led us to presuppose that proteins …

Fluorine-containing amino acids are valuable probes for the biophysical characterization of
proteins. Current methods for 19F-labeled protein production involve time-consuming …

Amyloid formation typically follows a time course in which there is a long lag period followed
by a rapid formation of fibrils. In this review, I show that the standard mechanisms of …

Oligomeric α-synuclein (αS) is considered to be the potential toxic species responsible for
the onset and progression of Parkinson's disease, possibly through the disruption of lipid …

Herein we describe a method for the efficient production (∼ 90% fluorination) of 5-F-Trp
human H ferritin via the selective incorporation of 19 F into the side chain of W93 using 5 …

Fibrils of the intrinsically disordered protein α-synuclein are hallmarks of Parkinson's
disease. The fluorescent dye thioflavin T is often used to characterize fibrillation, but this …

Understanding how environmental factors affect the conformational dynamics of α-synuclein
(α-syn) is of great importance because the accumulation and deposit of aggregated α-syn in …

Due to advances in methods for site-specific incorporation of unnatural amino acids (UAAs)
into proteins, a large number of UAAs with tailored chemical and/or physical properties have …

Traditionally, the biological fluorination of complex biological systems like proteins is
achieved through substitution of canonical amino acids or addition of fluorinated amino …