Zobrazeno 1 - 10
of 324
pro vyhledávání: '"Wand Aj"'
Publikováno v:
Biochemistry. 40:14744-14753
Oxidized flavodoxin from Cyanobacterium anabaena PCC 7119 is used as a model system to investigate the fast internal dynamics of a flavin-bearing protein. Virtually complete backbone and side chain resonance NMR assignments of an oxidized flavodoxin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e3866aabd9b98beddc7b4225cdb1638
https://doi.org/10.1021/bi011073d
https://doi.org/10.1021/bi011073d
Autor:
Wand Aj
Publikováno v:
Nature Structural Biology. 8:926-931
Recent developments in solution NMR methods have allowed for an unprecedented view of protein dynamics. Current insights into the nature of protein dynamics and their potential influence on protein structure, stability and function are reviewed. Part
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd29e9172bf82182b69c47b662ae59b9
https://doi.org/10.1038/nsb1101-926
https://doi.org/10.1038/nsb1101-926
Publikováno v:
Biochemistry. 40:6559-6569
A detailed characterization of the main chain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of methyl group resonances is presented. (15)N relaxation measurements confirm earlier results indicating tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d89ebf06255f6ee0436a9f8a00c7f3fb
https://doi.org/10.1021/bi0102252
https://doi.org/10.1021/bi0102252
Publikováno v:
Journal of the American Chemical Society. 121:4952-4960
An iterative redesign protocol for the transformation of a non-native peptide into a series of nativelike proteins derived from elementary considerations of biological evolution coupled with 1H NMR as an artificial selection criterion is presented. E
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e0a23f2ae127029c43b87ea2df0bacd
https://doi.org/10.1021/ja9833117
https://doi.org/10.1021/ja9833117
Publikováno v:
Journal of Biomolecular NMR. 14:75-78
The majority of proteins are too large to be comprehensively examined by solution NMR methods, primarily because they tumble too slowly in solution. One potential approach to making the NMR relaxation properties of large proteins amenable to modern s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::151e4c635a97050707563eb3eaebca48
https://doi.org/10.1023/a:1008354507250
https://doi.org/10.1023/a:1008354507250
Autor:
Ernesto J. Fuentes, Wand Aj
Publikováno v:
Biochemistry. 37:9877-9883
Hydrostatic pressure is used to perturb the manifold of states available to apocytochrome b562 and to examine the energetics and dynamics of the protein using hydrogen exchange monitored in real-time by heteronuclear spectroscopy at pressures ranging
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f749aeecb4ed390f340c03b5fb5091
https://doi.org/10.1021/bi980894o
https://doi.org/10.1021/bi980894o
Publikováno v:
Journal of the American Chemical Society. 120:3881-3886
A uniquely structured 65 amino acid helix−loop−helix‘−loop−helix‘‘ three-α-helix bundle, α3-1, was designed and chemically synthesized, using the crystallographically characterized three stranded c...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f1c284d65670e6601f72723085832c6b
https://doi.org/10.1021/ja973538m
https://doi.org/10.1021/ja973538m
Publikováno v:
Journal of Biomolecular NMR. 9:437-440
Selective incorporation of 13C into the methyl groupsof protein side chains is described as a means for simplifying themeasurement and interpretation of 13C relaxation parameters.High incorporation (>90%) is accomplished by using pyruvate(3-13C, 99%)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::28c433b6bc17e0c5d3521b766132e027
https://doi.org/10.1023/a:1018311013338
https://doi.org/10.1023/a:1018311013338
Publikováno v:
Biochemistry. 35:12275-12286
A model for the solution structure of horse heart ferricytochrome c has been determined by nuclear magnetic resonance spectroscopy combined with hybrid distance geometry-simulated annealing calculations. Forty-four highly refined structures were obta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::568e763b6a4d9f3d79cc8608d080ef59
https://doi.org/10.1021/bi961042w
https://doi.org/10.1021/bi961042w
Publikováno v:
Journal of the American Chemical Society. 128(45)
We show that a single internal polar interaction per helix is sufficient to engender structural specificity in that helix in helical bundle proteins. Furthermore, we use histidine-binding cofactors of different shapes which bind directly into the cor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89f300746231659f0987041bf5dcb543
https://pubmed.ncbi.nlm.nih.gov/17090015
https://pubmed.ncbi.nlm.nih.gov/17090015