Results 191 to 200 of about 18,838 (278)
The Importance of Being Imperfect: Structure and Function of Bacterial Amyloid. [PDF]
Peña-Díaz S +12 more
europepmc +1 more source
Proteinvermittelte Kupfer‐Redoxregulation: Rolle von Disulfidbrücken und allosterischer Modulation
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann +9 more
wiley +1 more source
Structural and morphological dynamics of "on-path" and "off-path" oligomers of human islet amyloid polypeptide. [PDF]
Warren D, Sitton J, Kurouski D.
europepmc +1 more source
The intrinsically disordered region of the human parathyroid hormone controls functional amyloid properties. [PDF]
Sachan S +7 more
europepmc +1 more source
Diese Studie beschreibt die Herstellung und Eigenschaften einer neuen Familie von o‐Terphenyl‐basierten Makrozyklen, TP[n] (n = 2‐8). Der Trimer bindet Phenylalanin in Wasser sehr effizient und ist dabei zehnmal selektiver als bei anderen Aminosäuren und aromatischen Neurotransmittern.
Swapnil Ghule +5 more
wiley +1 more source
Structural basis for T-cell intracellular antigen-1 amyloid fibril formation revealed by cryo-electron microscopy. [PDF]
Inaoka D +13 more
europepmc +1 more source
Origin of class B J-domain proteins involved in amyloid transactions. [PDF]
Domanski P +13 more
europepmc +1 more source
Copper binding triggers structural changes that expose a reactive disulphide bridge, enabling intrinsic Cu(II) reduction in folded proteins. SAXS, XAS, and QM/MM simulations reveal how globular proteins such as HSA and SOD1 employ disulphide‐mediated dynamics to modulate site accessibility and control copper redox chemistry.
Rebecca Sternke‐Hoffmann +9 more
wiley +1 more source

