Results about: protein structure
The findings of an IRB Barcelona study challenge a scientific principle about amyloid beta, a protein linked to Alzheimer’s disease
Natàlia Carulla’s research group provides information that questions the widely accepted premise regarding the number of molecules and the shape of the first aggregates formed by amyloid beta protein
Amyloid beta protein aggregation, the process by which molecules of this protein adhere to each other is strongly associated with the development of Alzheimer’s disease
Carulla’s work ultimately seeks to identify molecules that interfere with the initial stages of aggregation as a strategy to combat the disease.
Technology can now extend the album of 3D “photos” of membrane proteins, which currently covers 3% of these molecules
30% of human proteins exert their function in cell membranes and more than 50% act on these proteins.
New high-resolution microscopes and 3D calculation programmes are crucial to increase the number of atomic structures available, which currently stands at 440, this figure representing 3% of the estimated 15,000 that exist.
Today sees the start of a three-day conference in Barcelona involving 150 international scientists invited by the BBVA Foundation and IRB Barcelona.
Researchers at IRB and IBMB-CSIC, in Barcelona, and at the University of Wageningen, in the Netherlands, reveal how auxin hormone-regulated proteins activate developmental genes in plants.
Auxins are key components of plant growth and have many applications in agriculture. The biomedical application of these hormones are also being addressed.
The study is published this week in the scientific journal Cell.
IRB Barcelona scientists pave the way towards describing the conformation of proteins that do not have a defined structure
Structural and theoretical techniques are combined to develop new methodologies for the analysis of proteins