Zobrazeno 1 - 10
of 246
pro vyhledávání: '"S. RACKOVSKY"'
Publikováno v:
TASK Quarterly, Vol 18, Iss 3 (2014)
The need to interpret experimental results led to, first, an all-atom force field, followed by a coarse-grained one. As an aid to these force fields, a new approach is introduced here to predict protein structure based on the physical properties of t
Externí odkaz:
https://doaj.org/article/c754e60d6d7549e69f9864f4e159c57a
Akademický článek
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Autor:
S. Rackovsky, Harold A. Scheraga
Publikováno v:
Biopolymers
Using bioinformatic methods for treating protein dynamics, developed in earlier work, we study the relationship between sequence mobility and dynamics in proteins. It is shown that sequence mobility drives a transition between two dynamic regimes in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ff7c7ecf34d7aca47c165e5369465b5
https://doi.org/10.1002/bip.23411
https://doi.org/10.1002/bip.23411
Publikováno v:
The journal of physical chemistry. B. 124(46)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0617597122d13035f7384c8bf681c205
https://pubmed.ncbi.nlm.nih.gov/33095009
https://pubmed.ncbi.nlm.nih.gov/33095009
Autor:
Harold A. Scheraga, S. Rackovsky
Publikováno v:
Proc Natl Acad Sci U S A
We use a bioinformatic description of amino acid dynamic properties, based on residue-specific average B factors, to construct a dynamics-based, large-scale description of a space of protein sequences. We examine the relationship between that space a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d4b1ce382c2b98d1cfae442bdcb8f78
https://europepmc.org/articles/PMC7443874/
https://europepmc.org/articles/PMC7443874/
Autor:
S. Rackovsky, Harold A. Scheraga
Publikováno v:
Proteins
We examine the local and global properties of the average B-factor, 〈B〉, as a residue-specific indicator of protein dynamic characteristics. It has been shown that values of 〈B〉 for the 20 amino acids differ in a statistically significant man
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c1e0728e51dbd31923bc24d4ca6bbe0
https://europepmc.org/articles/PMC6718326/
https://europepmc.org/articles/PMC6718326/
Autor:
S, Rackovsky
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 1958
Traditional approaches to sequence alignment are based on evolutionary ideas. As a result, they are prebiased toward results which are in accord with initial expectations. We present here a method of sequence alignment which is based entirely on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::17be06258c8a6ea316d5a489bb050a9b
https://pubmed.ncbi.nlm.nih.gov/30945228
https://pubmed.ncbi.nlm.nih.gov/30945228
Autor:
S. Rackovsky
Publikováno v:
Methods in Molecular Biology ISBN: 9781493991600
Traditional approaches to sequence alignment are based on evolutionary ideas. As a result, they are prebiased toward results which are in accord with initial expectations. We present here a method of sequence alignment which is based entirely on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7cc77d26083d4654273ca153c1ef20f
https://doi.org/10.1007/978-1-4939-9161-7_18
https://doi.org/10.1007/978-1-4939-9161-7_18
Autor:
S. Rackovsky
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 83:1923-1928
We examine the utility of informatic-based methods in computational protein biophysics. To do so, we use newly developed metric functions to define completely independent sequence and structure spaces for a large database of proteins. By investigatin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::612ecd71ca416a2148a32c68f0be5ff3
https://doi.org/10.1002/prot.24916
https://doi.org/10.1002/prot.24916
Publikováno v:
Proceedings of the National Academy of Sciences. 112:5029-5032
The relationship between protein sequence and structure arises entirely from amino acid physical properties. An alternative method is therefore proposed to identify homologs in which residue equivalence is based exclusively on the pairwise physical p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bb50ffbdd5294a51346498068614cc37
https://doi.org/10.1073/pnas.1504806112
https://doi.org/10.1073/pnas.1504806112