Zobrazeno 1 - 10
of 4 959
pro vyhledávání: '"Daggett V"'
Autor:
Chen A; AltPep Corporation, 1150 Eastlake Avenue N, Suite 800, Seattle, WA, 98109, USA., Shea D; AltPep Corporation, 1150 Eastlake Avenue N, Suite 800, Seattle, WA, 98109, USA.; University of Washington, Box 355610, Seattle, WA, 98195-5610, USA., Daggett V; AltPep Corporation, 1150 Eastlake Avenue N, Suite 800, Seattle, WA, 98109, USA. daggett@uw.edu.; University of Washington, Box 355610, Seattle, WA, 98195-5610, USA. daggett@uw.edu.
Publikováno v:
Scientific reports [Sci Rep] 2024 Apr 04; Vol. 14 (1), pp. 7946. Date of Electronic Publication: 2024 Apr 04.
Autor:
Prosswimmer T; Molecular Engineering Program, University of Washington, Seattle, WA, 98195-5610, USA., Heng A; Department of Neuroscience, University of Washington, Seattle, WA, 98195-5610, USA.; Department of Biochemistry, University of Washington, Seattle, WA, 98195-5610, USA., Daggett V; Molecular Engineering Program, University of Washington, Seattle, WA, 98195-5610, USA. daggett@uw.edu.; Department of Biochemistry, University of Washington, Seattle, WA, 98195-5610, USA. daggett@uw.edu.; Department of Bioengineering, University of Washington, Seattle, WA, 98195-5610, USA. daggett@uw.edu.
Publikováno v:
Scientific reports [Sci Rep] 2024 Mar 05; Vol. 14 (1), pp. 5376. Date of Electronic Publication: 2024 Mar 05.
Yes
Molecular dynamics (MD) simulations contain considerable information with regard to the motions and fluctuations of a protein, the magnitude of which can be used to estimate conformational entropy. Here we survey conformational entropy acros
Molecular dynamics (MD) simulations contain considerable information with regard to the motions and fluctuations of a protein, the magnitude of which can be used to estimate conformational entropy. Here we survey conformational entropy acros
Externí odkaz:
http://hdl.handle.net/10454/13021
Autor:
Prosswimmer T; Molecular Engineering Program, University of Washington, Seattle, WA 98195, USA., Nick SE; Department of Bioengineering, University of Washington, Seattle, WA 98195, USA., Bryers JD; Department of Bioengineering, University of Washington, Seattle, WA 98195, USA., Daggett V; Molecular Engineering Program, University of Washington, Seattle, WA 98195, USA.; Department of Bioengineering, University of Washington, Seattle, WA 98195, USA.
Publikováno v:
International journal of molecular sciences [Int J Mol Sci] 2024 Jun 27; Vol. 25 (13). Date of Electronic Publication: 2024 Jun 27.
Autor:
Childers MC; Department of Bioengineering, University of Washington, Seattle, WA, USA., Daggett V; Department of Bioengineering, University of Washington, Seattle, WA, USA. daggett@uw.edu.
Publikováno v:
Methods in molecular biology (Clifton, N.J.) [Methods Mol Biol] 2023; Vol. 2552, pp. 109-124.
Autor:
Towse, Clare-Louise, Daggett, V.
This chapter gives an introduction to protein simulation methodology aimed at experimentalists and graduate students new to in silico investigations. More emphasis is placed on the knowledge needed to select appropriate simulation protocols, leaving
Externí odkaz:
http://hdl.handle.net/10454/11549
Autor:
Hsu CC; Department of Bioengineering, University of Washington, Seattle, Washington, USA.; Molecular Engineering Program, University of Washington, Seattle, Washington, USA., Templin AT; Division of Metabolism, Endocrinology and Nutrition, Department of Medicine, VA Puget Sound Health Care System and University of Washington, Seattle, Washington, USA., Prosswimmer T; Molecular Engineering Program, University of Washington, Seattle, Washington, USA., Shea D; Molecular Engineering Program, University of Washington, Seattle, Washington, USA., Li J; Department of Biochemistry, University of Washington, Seattle, Washington, USA., Brooks-Worrell B; Division of Metabolism, Endocrinology and Nutrition, Department of Medicine, VA Puget Sound Health Care System and University of Washington, Seattle, Washington, USA., Kahn SE; Division of Metabolism, Endocrinology and Nutrition, Department of Medicine, VA Puget Sound Health Care System and University of Washington, Seattle, Washington, USA., Daggett V; Department of Bioengineering, University of Washington, Seattle, Washington, USA.; Molecular Engineering Program, University of Washington, Seattle, Washington, USA.; Department of Biochemistry, University of Washington, Seattle, Washington, USA.
Publikováno v:
Protein science : a publication of the Protein Society [Protein Sci] 2024 Feb; Vol. 33 (2), pp. e4854.
The conformational propensities of amino acids are an amalgamation of sequence effects, environmental effects and underlying intrinsic behavior. Many have attempted to investigate neighboring residue effects to aid in our understanding of protein fol
Externí odkaz:
http://hdl.handle.net/10454/11432
Various host-guest peptide series are used by experimentalists as reference conformational states. One such use is as a baseline for random-coil NMR chemical shifts. Comparison to this random-coil baseline, through secondary chemical shifts, is used
Externí odkaz:
http://hdl.handle.net/10454/11545
Most rotamer libraries are generated from subsets of the PDB and do not fully represent the conformational scope of protein side chains. Previous attempts to rectify this sparse coverage of conformational space have involved application of weighting
Externí odkaz:
http://hdl.handle.net/10454/11546