Intellectual property management at the National Animal Science Research Institute in India: A case study.

Aim: The National Institute of Veterinary Epidemiology and Disease Informatics is an animal science research institute under the aegis of the Indian Council of Agricultural Research. The intellectual property management system (IPMS) of the institute oversees technology creation, protection, and transfer/commercialization. This study reviews the effectiveness of the IPMS using traditional strengths, weaknesses, opportunities, and threats (SWOT) evaluation.

Hydrogen bonds are a primary driving force for de novo protein folding. Corrigendum.

The paper by Lee et al. [(2017). Acta Cryst.

Unwinding of the Substrate Transmembrane Helix in Intramembrane Proteolysis.

Intramembrane-cleaving proteases (I-CLiPs) activate pools of single-pass helical membrane protein signaling precursors that are key in the physiology of prokaryotic and eukaryotic cells. Proteases typically cleave peptide bonds within extended or flexible regions of their substrates, and thus the mechanism underlying the ability of I-CLiPs to hydrolyze the presumably α-helical transmembrane domain (TMD) of these membrane proteins is unclear. Using deep-ultraviolet resonance Raman spectroscopy in combination with isotopic labeling, we show that although predominantly in canonical α-helical conformation, the TMD of the established I-CLiP substrate Gurken displays 3-helical geometry.

Hydrogen bonds are a primary driving force for de novo protein folding.

The protein-folding mechanism remains a major puzzle in life science. Purified soluble activation-induced cytidine deaminase (AID) is one of the most difficult proteins to obtain. Starting from inclusion bodies containing a C-terminally truncated version of AID (residues 1-153; AID), an optimized in vitro folding procedure was derived to obtain large amounts of AID, which led to crystals with good quality and to final structural determination.

A New Method to Determine the Transmembrane Conformation of Substrates in Intramembrane Proteolysis by Deep-UV Resonance Raman Spectroscopy.

We present a new method based on deep-UV resonance Raman spectroscopy to determine the backbone conformation of intramembrane protease substrates. The classical amide vibrational modes reporting on the conformation of just the transmembrane region of the substrate can be resolved from solvent exchangeable regions outside the detergent micelle by partial deuteration of the solvent. In the presence of isotopically triple-labeled intramembrane protease, these amide modes can be accurately measured to monitor the transmembrane conformation of the substrate during intramembrane proteolysis.