Chemical shifts are the mileposts of NMR. For more than 60 years [1, 2], they have been
used by chemists as highly reproducible, easily measured parameters to map out the …

Proteins are dynamic entities, and they possess an inherent flexibility that allows them to
function through molecular interactions within the cell, among cells and even between …

The automated assignment of NOESY cross peaks has become a fundamental technique for
NMR protein structure analysis. A widely used algorithm for this purpose is implemented in …

Induced oncoproteins degradation provides an attractive anti-cancer modality. Activation of
anaphase-promoting complex (APC/CCDH1) prevents cell-cycle entry by targeting crucial …

Transactive response DNA‐binding protein 43 kDa (TDP‐43) is an RNA transporting and
processing protein whose aberrant aggregates are implicated in neurodegenerative …

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a
stable three-dimensional structure, but rather adopt many different conformations in dynamic …

The aggregation of the microtubule-associated protein tau into paired helical filaments to
form neurofibrillary tangles constitutes one of the pathological hallmarks of Alzheimer's …

Autoinhibition is being widely used in nature to repress otherwise constitutive protein
activities and is typically regulated by extrinsic factors. Here we show that autoinhibition can …

Every year between 500 and 1000 peptide and protein structures are determined by NMR
and deposited into the Protein Data Bank. However, the process of NMR structure …

We present a program, named Promega, to predict the Xaa-Pro peptide bond conformation
on the basis of backbone chemical shifts and the amino acid sequence. Using a chemical …