Results 91 to 100 of about 3,587,930 (291)

Elucidating ATP’s role as solubilizer of biomolecular aggregate

eLife
Proteins occurring in significantly high concentrations in cellular environments (over 100 mg/ml) and functioning in crowded cytoplasm, often face the prodigious challenges of aggregation which are the pathological hallmark of aging and are critically ...
Susmita Sarkar, Saurabh Gupta, Chiranjit Mahato, Dibyendu Das, Jagannath Mondal   +4 more
doaj   +1 more source

Evaluation of sequence features from intrinsically disordered regions for the estimation of protein function.

PLoS ONE, 2014
With the exponential increase in the number of sequenced organisms, automated annotation of proteins is becoming increasingly important. Intrinsically disordered regions are known to play a significant role in protein function.
Alok Sharma, Abdollah Dehzangi, James Lyons, Seiya Imoto, Satoru Miyano, Kenta Nakai, Ashwini Patil   +6 more
doaj   +1 more source

Functional Diversity and Structural Disorder in the Human Ubiquitination Pathway [PDF]

, 2013
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and several
Mainak Guharoy, Rita Pancsa (173029), Pallab Bhowmick, Tompa, Péter, Pallab Bhowmick (416342), Peter Tompa, Bhowmick, Pallab, Pancsa Rita, Guharoy Mainak, Bhowmick Pallab, Tompa Peter, Guharoy, Majnak, Mainak Guharoy (416343), Peter Tompa (38445), Rita Pancsa, Pancsa, Rita   +15 more
core   +1 more source

Smaller is better: nanobodies meet NMR

FEBS Letters, EarlyView.
Nanobodies are single‐domain antigen‐binding fragments derived from camelid heavy chain antibodies. Their small size, high stability, and exceptional specificity make nanobodies uniquely useful probes for NMR studies of protein dynamics, transient conformational states, and protein–protein interactions.
Oleg Y. Dmitriev
wiley   +1 more source

SCREENING INTERACTIONS BETWEEN PROTEINS AND DISORDERED PEPTIDES BY A NOVEL COMPUTATIONAL METHOD [PDF]

, 2013
Concerted interactions between proteins in cells form the basis of most biological processes. Biophysicists study protein–protein association by measuring thermodynamic and kinetic properties.
Zhang, Weiyi
core  

Invisible but not inaccessible—Revealing transient oligomers formed by intrinsically disordered proteins with solution NMR and complementary methods

FEBS Letters, EarlyView.
Transient oligomers formed by intrinsically disordered proteins may be ‘invisible’ to direct detection yet remain accessible to solution NMR through equilibrium‐exchange measurements and pressure‐jump experiments. Complementary methods report on mass, stoichiometry, selected distance distributions, morphology, and internal packing.
Martin D. Gelenter, Ad Bax
wiley   +1 more source

Zero-shot segmentation using embeddings from a protein language model identifies functional regions in the human proteome.

PLoS Computational Biology
The biological function of a protein is often determined by its distinct functional units, such as folded domains and intrinsically disordered regions.
Ami G Sangster, Cameron Dufault, Haoning Qu, Denise Le, Julie D Forman-Kay, Alan M Moses   +5 more
doaj   +1 more source

Membrane composition and thermodynamic identity as boundaries of life for synthetic cell research

FEBS Letters, EarlyView.
What makes a cell a cell? The boundary of a living cell is not just a wall. Read as a Markov blanket, the membrane separates internal from external states, generating identity and non‐equilibrium order. Can this identity be rebuilt from scratch in a synthetic cell?
Caterina Presutti, Bert Poolman
wiley   +1 more source

Fine structures of intrinsically disordered proteins

The Journal of Chemical Physics
We report simulation studies of 33 single intrinsically disordered proteins (IDPs) using coarse-grained bead-spring models where interactions among different amino acids are introduced through a hydropathy matrix and additional screened Coulomb interaction for the charged amino acid beads. Our simulation studies of two different hydropathy scales (HPS1,
Swarnadeep Seth, Brandon Stine, Aniket Bhattacharya   +2 more
openaire   +3 more sources

Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq [PDF]

, 2011
The hexameric Escherichia coli RNA chaperone Hfq (Hfq(Ec)) is involved in riboregulation of target mRNAs by small trans-encoded RNAs. Hfq proteins of different bacteria comprise an evolutionarily conserved core, whereas the C-terminus is variable in ...
Beich-Frandsen, Mads (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Kontaxis, Georg (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Blasi, U., Rajkowitsch, L., Miles, Andrew (Birkbeck College), Sjöblom, Björn (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Miles, Andrew J., Svergun, D.I., Kloiber, K., Kristina Djinović-Carugo, Vecerek, B., Karin Kloiber, Konarev, P.V., Lukas Rajkowitsch, Hämmerle, Hermann Konrad (Department of Biochemistry and Cell Biology, Centre for Molecular Biology, University of Vienna), Georg Kontaxis, Bläsi, Udo (Department of Microbiology, Immunobiology and Genetics, Centre for Molecular Biology, University of Vienna), Djinovic-Carugo, K., Robert Konrat, Branislav Večerek, Konarev, Peter V. (EMBL Hamburg), Andrew J. Miles, Kloiber, Karin (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Rajkowitsch, Lukas (Department of Biochemistry and Cell Biology, Centre for Molecular Biology, University of Vienna), Udo Bläsi, Wallace, Bonnie A., Svergun, D. I., Petr V. Konarev, Svergun, Dimitri I. (EMBL Hamburg), Björn Sjöblom, Hammerle, H., Mads Beich-Frandsen, Wallace, B. A., Sjoblom, B., Miles, A. J., Konrat, Robert (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Vecerek, Branislav (Department of Microbiology, Immunobiology and Genetics, Centre for Molecular Biology, University of Vienna), Dimitri I. Svergun, B. A. Wallace, Beich Frandsen, M., Djinovic Carugo, K., Konarev, P. V., Beich-Frandsen, M., Konrat, R., Djinovic-Carugo, Kristina (Department of Structural and Computational Biology, Centre for Molecular Biology, University of Vienna), Hermann Hämmerle, Kontaxis, G.   +46 more
core   +1 more source