Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Matthew, Revington"'
Publikováno v:
The Journal of Organic Chemistry. 81:2981-2986
N,N'-Diacyl bispidines exhibit chirality in the absence of a chiral center and axis. Conformational analysis indicates planar chirality in the molecular structure as a result of open-ended chiral planes, which has been confirmed by X-ray diffraction
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b583e8d74adf6bc30aeaa170ddee396b
https://doi.org/10.1021/acs.joc.6b00250
https://doi.org/10.1021/acs.joc.6b00250
Publikováno v:
Journal of Magnetic Resonance. 203:11-28
A decade ago, Dr. L.E. Kay and co-workers described an ingenious HNCO-based triple-resonance experiment from which several protein backbone RDCs can be measured simultaneously (Yang et al. (1999) [1] ). They implemented a J-scaling technique in the 1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4dea17eb50a6835155c1e05efd66e5a9
https://doi.org/10.1016/j.jmr.2009.11.014
https://doi.org/10.1016/j.jmr.2009.11.014
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 73:28-42
S100B is one of the best-characterized members of the calcium-signaling S100 protein family. Most S100 proteins are dimeric, with each monomer containing two EF-hand calcium-binding sites (EF1, EF2). S100B and other S100 proteins respond to calcium i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c1a43a12176ec3965e6b5a9dec918db
https://doi.org/10.1002/prot.22037
https://doi.org/10.1002/prot.22037
Publikováno v:
Journal of Biomolecular NMR. 35:295-300
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0850b104b5f90362b9010e7a168d54ba
https://doi.org/10.1007/s10858-006-9032-y
https://doi.org/10.1007/s10858-006-9032-y
Publikováno v:
Protein Science. 14:3115-3120
YdhR is a 101-residue conserved protein from Escherichia coli. Sequence searches reveal that the protein has >50% identity to proteins found in a variety of other bacterial genomes. Using size exclusion chromatography and fluorescence spectroscopy, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a20d864c2ee44ac866d182e35c9007db
https://doi.org/10.1110/ps.051809305
https://doi.org/10.1110/ps.051809305
Autor:
Alexander V. Kurochkin, Matthew Revington, Yongbo Zhang, Erik R. P. Zuiderweg, Groverv N.B. Yip
Publikováno v:
Journal of Molecular Biology. 349:163-183
Hsp70 chaperones are two-domain proteins that assist in intra-cellular protein (re) folding processes in all species. The protein folding activity of the substrate binding domain of the Hsp70s is regulated by nucleotide binding at the nucleotide-bind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8bff5aa5cc795aac46c077ae5ccfe643
https://doi.org/10.1016/j.jmb.2005.03.033
https://doi.org/10.1016/j.jmb.2005.03.033
Publikováno v:
Journal of Biological Chemistry. 279:33958-33967
We present an NMR investigation of the nucleotide-dependent conformational properties of a 44-kDa nucleotide binding domain (NBD) of an Hsp70 protein. Conformational changes driven by ATP binding and hydrolysis in the N-terminal NBD are believed to a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e911d95e358beb23d75a4032e232ac24
https://doi.org/10.1074/jbc.m313967200
https://doi.org/10.1074/jbc.m313967200
Publikováno v:
Protein Science. 11:1227-1238
The F(1)F(0) ATP synthase is a reversible molecular motor that employs a rotary catalytic cycle to couple a chemiosmotic membrane potential to the formation/hydrolysis of ATP. The multisubunit enzyme contains two copies of the b subunit that form a h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c322a00ed06a8c832f8b5cd6f7f2ae2
https://doi.org/10.1110/ps.3200102
https://doi.org/10.1110/ps.3200102
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459:521-527
The effects of mutation of residue Ala-128 of the b subunit of Escherichia coli ATP synthase to aspartate on the structure of the subunit and its interaction with the F1 sector were analyzed. Determination of solution molecular weights by sedimentati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb7f161e29729e77953f4de0011e6541
https://doi.org/10.1016/s0005-2728(00)00192-4
https://doi.org/10.1016/s0005-2728(00)00192-4
Publikováno v:
Journal of Bioenergetics and Biomembranes. 32:347-355
The b subunit of ATP synthase is a major component of the second stalk connecting the F1and F0 sectors of the enzyme and is essential for normal assembly and function. The156-residue b subunit of the Escherichia coli ATP synthase has been investigate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::01061c20a8ddf08bbdf8212d30b1c848
https://doi.org/10.1023/a:1005571818730
https://doi.org/10.1023/a:1005571818730