Results 51 to 60 of about 181,206 (262)

Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria

Bioscience Reports, 2013
The autosomal dominantly inherited disease AIP (acute intermittent porphyria) is caused by mutations in HMBS [hydroxymethylbilane synthase; also known as PBG (porphobilinogen) deaminase], the third enzyme in the haem biosynthesis pathway.
Aurora Martinez, Karen Toska, Helene J. Bustad, Marta Vorland, Eva Rønneseth, Sverre Sandberg   +5 more
doaj   +1 more source

Protease-sensitive conformers in broad spectrum of distinct PrPSc structures in sporadic Creutzfeldt-Jakob disease are indicator of progression rate. [PDF]

PLoS Pathogens, 2011
The origin, range, and structure of prions causing the most common human prion disease, sporadic Creutzfeldt-Jakob disease (sCJD), are largely unknown.
Chae Kim, Tracy Haldiman, Yvonne Cohen, Wei Chen, Janis Blevins, Man-Sun Sy, Mark Cohen, Jiri G Safar   +7 more
doaj   +1 more source

Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates

FEBS Letters, EarlyView.
Inositol pyrophosphates are energy‐rich signaling molecules that perform critical functions in cells. Three different families of phosphatases hydrolyze the β phosphate of the inositol pyrophosphate molecules: two have narrow specificities and one is promiscuous.
Ronda J. Rolfes
wiley   +1 more source

Dissecting the Conformational Stability of a Glycan Hairpin

Journal of the American Chemical Society
Systematic structural studies of model oligopeptides revealed important aspects of protein folding and offered design principles to access non-natural materials. In the same way, the rules that regulate glycan folding could be established by studying synthetic oligosaccharide models.
Yadav, Nishu, Djalali, Surusch, Poveda, Ana, Ricardo, Manuel G., Seeberger, Peter H., Jiménez-Barbero, Jesús, Delbianco, Martina   +6 more
openaire   +3 more sources

Conformational stability of adrenodoxin mutant proteins [PDF]

Protein Science, 1996
AbstractAdrenodoxin and the mutants at the positions T54, H56, D76, Y82, and C95, as well as the deletion mutants 4–114 and 4–108, were studied by high‐sensitivity scanning microcalorimetry, limited proteolysis, and absorption spectroscopy. The mutants show thermal transition temperatures ranging from 46 to 56 °C, enthalpy changes from 250 to 370 kJ ...
Pfeil, Wolfgang, Burova, Tatjana V., Beckert, Vita, Uhlmann, Heike, Ristau, Otto, Bernhardt, Rita   +5 more
openaire   +4 more sources

Reconstructing enzyme evolution by protein engineering

FEBS Letters, EarlyView.
Natural enzyme evolution can be retraced by protein engineering methods such as directed evolution, rational design, and ancestral sequence reconstruction. These approaches reveal how enzymes emerged from ligand‐binding scaffolds, developed varying substrate preferences, formed oligomeric complexes, adapted to environmental changes, and evolved novel ...
Lukas Drexler, Markus R. Busch, Reinhard Sterner   +2 more
wiley   +1 more source

Identification of a Shiga toxin A‐derived peptide internalized into Gb3 receptor‐bearing cells via interaction with the Shiga toxin B subunit

FEBS Letters, EarlyView.
The process of internalization of the Shiga toxin A subunit via formation of a complex with the Shiga toxin B subunit, which specifically binds to the Gb3 receptor. The peptide is designed to act as a carrier of drugs into cancer cells. Here, we explored the potential of peptides derived from the catalytic A subunit of Shiga toxin (STxA) to be drug ...
Giulia Opassi, João C. Encarnação, Valeria Napolitano, Grzegorz Dubin, Grzegorz Popowicz, Karl Andersson, U. Helena Danielson   +6 more
wiley   +1 more source

The Mechanism of Conformational Transition and Stabilisation Strategies of Viral Membrane Fusion Proteins

Shengwu huaxue yu shengwu wuli jinzhan
Viral membrane fusion proteins facilitate the fusion of viral and host cell membranes by undergoing a transition from a prefusion conformation to a post-fusion conformation, thereby enabling the transfer of viral nucleic acids into the cell interior ...
XIE Chen-Yi, DONG Xiang-Ge, ZHAN Jiu-Yu, ZHU Hong-Wei, YU Xin, LIU Yang, YU Jia-Yu, ZHANG Xing-Xiao   +7 more
doaj   +1 more source

Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions

FEBS Letters, EarlyView.
The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang, Hyo Been Jin, Chang Min Kim, So Yeon Lee, Hyun Ho Park   +4 more
wiley   +1 more source

Conformational stability of porcine serum transferrin [PDF]

Protein Science, 1992
AbstractThe conformation of porcine serum ferric transferrin (Tf) and its stability against denaturation were studied by circular dichroism. Tf was estimated to have 19–24% α‐helix and 50–55% β‐sheet based on the methods of Chang et al. (Chang, C.T., Wu, C.‐S.C., & Yang, J.T., 1978, Anal. Biochem. 91, 13–31) and Provencher and Glöckner (Provencher,
Z M, Shen, J T, Yang, Y M, Feng, C S, Wu
openaire   +2 more sources