In the past 20 years protein and peptide self-assembly has attracted material scientists' interest due to the possibility to exploit such molecular mechanism to create novel biomaterials including hydrogels. One of the main challenges when dealing with "soft" biological materials is their structural and morphological characterisation. Small angle scattering (SAS) can be a highly complementary tool to microscopy for the characterisation of such materials as it allows the investigation of samples in their wet-state without the need for any sample preparation such as drying and/or freezing. In this tutorial review we introduce briefly the SAS technique to the non-expert and through selected examples from the literature show how SAS can be readily used thanks to existing analytical approaches developed by a number of authors to extract structural information on the self-assembly of peptide and proteins.
The effects of guanidinium hydrochloride (GdmCl) on two intrinsically disordered proteins (IDPs) are investigated using simulations of the self-organized polymer-IDP (SOP-IDP) model. The impact of GdmCl is taken into account using the molecular transfer model (MTM). We show that due to the dramatic reduction in the stiffness of the highly charged Prothymosin-α (ProTα) with increasing concentration of GdmCl ([GdmCl]), the radius of gyration () decreases sharply until about 1.
Cellulose nanocrystals (CNCs) are known to self-assemble into a left-handed chiral nematic lyotropic liquid crystalline phase in water. When captured in the solid state, this structure can impart films with photonic properties that make them promising candidates in photonics, sensing, security, and other areas. Unfortunately, the intrinsic hydrophilicity of CNCs renders these iridescent films susceptible to moisture, thereby limiting their practicality.
Monoclonal antibodies recognizing nonprotein antigens remain largely underrepresented in our understanding of the molecular repertoire of innate and adaptive immunity. One such antibody is Mannitou, a murine IgM that recognizes paucimannosidic glycans. In this work, we report the production and purification of the recombinant antigen-binding fragment (Fab) of Mannitou IgM (Mannitou Fab) and employ a combination of biochemical and biophysical approaches to obtain its initial structural characterization.
Energy correlators provide a powerful observable to study fragmentation dynamics in QCD. We demonstrate that the leading nonperturbative corrections for projected N-point energy correlators are described by the same universal parameter for any N, which has already been determined from other event shape fits. Including renormalon-free nonperturbative corrections substantially improves theoretical predictions of energy correlators, notably the transition into the confining region at small angles.
In recent years, energy correlators have emerged as a powerful tool to explore the field theoretic structure of strong interactions at particle colliders. In this Letter we initiate a novel study of the nonperturbative power corrections to the projected N-point energy correlators in the limit where the angle between the detectors is small. Using the light-ray operator product expansion as a guiding principle, we derive the power corrections in terms of two nonperturbative quantities describing the fragmentation of quarks and gluons.
