Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Nadine C. Gassner"'
Autor:
Arif Nukanto, Samarkand A. Estee, Karen Tenney, Atit Kanti, Joseline Ratnam, Johann Sohn, Heddy Julistiono, Yongchun Shen, Steven T. Loveridge, Nadine C. Gassner, Junke Liu, Helene C. Vervoort, Wayne D. Inman, Kyria Boundy-Mills, Leonard F. Bjeldanes, Leonardus B.S. Kardono, R. Scott Lokey, Tyler A. Johnson, Phillip Crews, Kenny K. H. Ang, James H. McKerrow, Walter M. Bray
Publikováno v:
Journal of Natural Products. 74:2545-2555
A high-throughput (HT) paradigm generating LC-MS-UV-ELSD-based natural product libraries to discover compounds with new bioactivities and or molecular structures is presented. To validate this methodology, an extract of the Indo-Pacific marine sponge
Autor:
Brandon I. Morinaka, Sarah J. Robinson, Joseph Media, Phillip Crews, Katharine R. Watts, Taro Amagata, Walter M. Bray, Nadine C. Gassner, R. Scott Lokey, Karen Tenney, Frederick A. Valeriote
Publikováno v:
Journal of Natural Products. 74:341-351
The cyclodepsipeptide jasplakinolide (1) (a.k.a. jaspamide), isolated previously from the marine sponge Jaspis splendens, is a unique cytotoxin and molecular probe that operates through stabilization of filamentous actin (F-actin). We have recently d
Autor:
Matt Massie, Nadine C. Gassner, Benedict Paten, Mark Diekhans, Barbara J. Wold, David Haussler, Stephen H. Friend, Justin Guinney, Adam A. Margolin, W. James Kent, Brian J. Druker, Maciej Smuga-Otto, Joshua M. Stuart, Laura J. van't Veer, Adam M. Novak, Lior Pachter, Mitchell Guttman, Frank Austin Nothaft, David A. Patterson, Patrick E. Mantey
Publikováno v:
Journal of the American Medical Informatics Association : JAMIA. 22(6)
The world’s genomics data will never be stored in a single repository – rather, it will be distributed among many sites in many countries. No one site will have enough data to explain genotype to phenotype relationships in rare diseases; therefor
Autor:
Brian W. Matthews, Blaine H. M. Mooers, Nadine C. Gassner, Michael L. Quillin, Robert D. Busam, Walter A. Baase, Joel D. Lindstrom, Larry H. Weaver
Publikováno v:
Biophysical Chemistry. 100:325-340
In order to further explore the tolerance of proteins to amino acid substitutions within the interior, a series of core residues was replaced by methionine within the C-terminal domain of T4 lysozyme. By replacing leucine, isoleucine, valine and phen
Autor:
Brian W. Matthews, Nadine C. Gassner
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:1967-1970
Using heavily methionine-substituted T4 lysozyme as an example, it is shown how the addition or deletion of a small number of methionines can simplify the location of selenium sites for use in MAD phasing. By comparing the X-ray data for a large numb
Publikováno v:
Journal of Molecular Biology. 294:17-20
The availability of a series of phage T4 lysozymes with up to 14 methionine residues incorporated within the protein has made it possible to systematically compare the effect on protein stability of selenomethionine relative to methionine. Wild-type
Autor:
Walter A. Baase, Frederick W. Dahlquist, Brian W. Matthews, Joel D. Lindstrom, Nadine C. Gassner, Jirong Lu
Publikováno v:
Biochemistry. 38:14451-14460
In an attempt to identify a systematic relation between the structure of a protein and its folding kinetics, the rate of folding was determined for 20 mutants of T4 lysozyme in which a bulky, buried, nonpolar wild-type residue (Leu, Ile, Phe, Val, or
Autor:
Aimee M. Eldridge, Walter A. Baase, Brain W. Matthews, Nadine C. Gassner, Sheila D. Snow, Devin L. Drew, Leigh Ann Lipscomb
Publikováno v:
Protein Science. 7:765-773
The substitution of methionines with leucines within the interior of a protein is expected to increase stability both because of a more favorable solvent transfer term as well as the reduced entropic cost of holding a leucine side chain in a defined
Publikováno v:
Proceedings of the National Academy of Sciences. 93:12155-12158
To test whether the structure of a protein is determined in a manner akin to the assembly of a jigsaw puzzle, up to 10 adjacent residues within the core of T4 lysozyme were replaced by methionine. Such variants are active and fold cooperatively with
Autor:
Nadine C. Gassner, John A. Schellman
Publikováno v:
Biophysical Chemistry. 59:259-275
G. Makhatadze and P. Privalov [J. Mol. Biol., 226 (1995) 491] have recently measured the enthalpy of transfer of three proteins into urea and guanidinium chloride solutions as a function of concentration and temperature. The present paper applies the