neuroserpin, a member of the serine proteinase inhibitor (serpin) superfamily, is known to be a neuroprotective factor in the focal ischemic stroke followed by reducing the microglial activation. neuroserpin is a protein rich of methionine residues that can scavenge the free radical species which may increase its neuroprotective effect. on the other hand, the oxidative modifications of the amin...

Research on change-point detection, the classical problem of detecting abrupt changes in sequential data, has focused predominantly on datasets with a single observable. A growing number of time series datasets, however, involve many observables, often with the property that a given change typically affects only a few of the observables. We introduce a general statistical method that, given man...

In the structure of the title salt [systematic name: 3-(10,11-dihydro-5H-dibenzo[a,d][7]annulen-5-ylidene)-N,N-dimethylpropan-1-aminium 2,4,6-trinitrophenolate] of a tricyclic antidepressant, C(20)H(24)N+.C(6)H(2)N(3)O(7)-, the dimethylaminopropyl subunit possesses a classical static conformational disorder. The central cycloheptadiene ring adopts a bent conformation that is intermediate betwee...

We have studied the temperature dependence of the absorption spectra of soluble, conjugated polymers of known chain length ~;100–1000 double bonds!, synthesized by Schattenmann et al. @Macromolecules 29, 8990 ~1996!# using living polymerization techniques. The polymer spectra show significant redshifts upon cooling from 300 to 80 K. To estimate the distributions of conjugated segments in these ...

Protein structure is commonly regarded to be conserved and to dictate function. Most proteins rely on conformational flexibility to some degree. Are regions that convey conformational flexibility conserved over evolutionary time? Can changes in conformational flexibility alter protein function? Here, the evolutionary dynamics of structurally ordered and disordered (flexible) regions are investi...

Though lacking a well-defined three-dimensional structure, intrinsically unstructured proteins are ubiquitous in nature. These molecules play crucial roles in many cellular processes, especially signaling and regulation. Surprisingly, even enzyme catalysis can tolerate substantial disorder. This observation contravenes conventional wisdom but is relevant to an understanding of how protein dynam...