Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Maya J. Pandya"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 5 (2018)
We have used NMR and computational methods to characterize the dynamics of the ribonuclease barnase over a wide range of timescales in free and inhibitor-bound states. Using temperature- and denaturant-dependent measurements of chemical shift, we sho
Externí odkaz:
https://doaj.org/article/36e10a5ca2514b99be6ec5e2bbc29727
Autor:
Stefanie Schiffers, Andrea M. Hounslow, Michael P. Williamson, Nicola J. Baxter, Maya J. Pandya
Publikováno v:
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences, Vol 5 (2018)
Frontiers in Molecular Biosciences, Vol 5 (2018)
We have used NMR and computational methods to characterize the dynamics of the ribonuclease barnase over a wide range of timescales in free and inhibitor-bound states. Using temperature- and denaturant-dependent measurements of chemical shift, we sho
Publikováno v:
Biophysical Journal. 97(5):1482-1490
In this work we measured 1H NMR chemical shifts for the ribonuclease barnase at pressures from 3 MPa to 200 MPa, both free and bound to d(CGAC). Shift changes with pressure were used as restraints to determine the change in structure with pressure. F
Publikováno v:
Biochemical Journal. 400:75-80
Tetrahydrobiopterin is an essential cofactor for aromatic amino acid hydroxylases, ether lipid oxidase and nitric oxide synthases. Its biosynthesis in mammals is regulated by the activity of the homodecameric enzyme GCH (GTP cyclohydrolase I; EC 3.5.
Publikováno v:
Smith, A, BANWELL, EF, EDWARDS, WR, PANDYA, MJ & WOOLFSON, DN 2006, ' Engineering increased stability into self-assembled protein fibers ', Advanced Functional Materials, vol. 16, no. 8, pp. 1022-1030 . https://doi.org/10.1002/adfm.200500568
Two stages in the rational redesign of a peptide-based, self-assembling fiber (SAF) are described. The SAF system comprises two peptides designed to form an offset a-helical coiled-coil heterodimer. The "sticky-ends" are complementary and promote lon
Autor:
Brett D. Welch, John M. Dye, Andrew S. Herbert, Frank G. Whitby, Christopher P. Hill, Tracy R. Clinton, Rena McKinnon, Debra M. Eckert, Michael S. Kay, Matthew T. Weinstock, Maya J. Pandya, Laura I. Prugar, Nicolas Szabo-Fresnais, Michael T. Jacobsen
Publikováno v:
Protein Science
Ebolaviruses are highly lethal filoviruses that cause hemorrhagic fever in humans and nonhuman primates. With no approved treatments or preventatives, the development of an anti-ebolavirus therapy to protect against natural infections and potential w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82d8a79955180f25285e4ad1e937ecda
https://europepmc.org/articles/PMC4380977/
https://europepmc.org/articles/PMC4380977/
Autor:
Gillian M. Spooner, Derek N. Woolfson, Julian R. Thorpe, Margaret Sunde, Maya J. Pandya, and Alison Rodger
Publikováno v:
Biochemistry. 39:8728-8734
Coiled-coil motifs provide simple systems for studying molecular self-assembly. We designed two 28-residue peptides to assemble into an extended coiled-coil fiber. Complementary interactions in the core and flanking ion-pairs were used to direct stag
Autor:
Peter R. Shewry, Maya J. Pandya, Anthony R. Clarke, Arthur S. Tatham, Christopher E. Dempsey, Richard B. Sessions, Phil B. Williams
Publikováno v:
Proteins: Structure, Function, and Genetics. 38:341-349
The 2 S seed storage protein, sunflower albumin 8, contains an unusually high proportion of hydrophobic residues including 16 methionines in a mature protein of 103 amino acids. A structural model, based on the known structure of a related protein, h
Publikováno v:
University of Bristol-PURE
The 2 S seed storage protein, sunflower albumin 8 (SFA-8), contains an unusually high proportion of hydrophobic residues including 16 methionines (some of which may form a surface hydrophobic patch) in a disulfide cross-linked, alpha-helical structur
Publikováno v:
Phytochemistry. 43:327-331
The major trypsin isoinhibitors from seed extracts of buckwheat (Fagopyrum esculentum Mönch) were purified by affinity chromatography, anion exchange chromatography, anion exchange HPLC and reversed-phase HPLC, and the complete amino acid sequences