Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Stefan J. Hamill"'
Autor:
Susan B. Fowler, Stefan J. Hamill, Jane Clarke, Ilkka Lappalainen, Benjamin Moore, Lucy G. Randles
Publikováno v:
Journal of Biological Chemistry. 281:24216-24226
It has proved impossible to purify some proteins implicated in disease in sufficient quantities to allow a biophysical characterization of the effect of pathogenic mutations. To overcome this problem we have analyzed 37 different disease-causing muta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d03e980cdf2a7ef73d35c7da33ef10c3
https://doi.org/10.1074/jbc.m603593200
https://doi.org/10.1074/jbc.m603593200
Publikováno v:
Journal of Molecular Biology. 295:641-649
What are the selective pressures on protein sequences during evolution? Amino acid residues may be highly conserved for functional or structural (stability) reasons. Theoretical studies have proposed that residues involved in the folding nucleus may
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d05b0b798ea6fb67fa3d553b2fd1508b
https://doi.org/10.1006/jmbi.1999.3360
https://doi.org/10.1006/jmbi.1999.3360
Publikováno v:
Journal of Molecular Biology. 282:181-194
The third fibronectin type III domain from human tenascin adopts a compact beta-sandwich fold. Its boundaries were originally selected to encode a 90-residue domain (TNfn31-90). We conclude that the dynamic properties of TNfn3 are more accurately rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e51776cd2b9ebb57c276bba008de09f
https://doi.org/10.1006/jmbi.1998.2019
https://doi.org/10.1006/jmbi.1998.2019
Autor:
Richard James, Wei Li, Andrew M. Hemmings, Colin Kleanthous, Geoffrey R. Moore, Stefan J. Hamill
Publikováno v:
Biochemistry. 37:11771-11779
The immunity protein Im2 can bind and inhibit the noncognate endonuclease domain of the bacterial toxin colicin E9 with a Kd of 19 nM, 6 orders of magnitude weaker than that of the cognate immunity protein Im9 with which it shares 68% sequence identi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be832247e29fb504430b9c47c259c6c3
https://doi.org/10.1021/bi9808621
https://doi.org/10.1021/bi9808621
Publikováno v:
Journal of molecular biology. 302(3)
As part of a systematic study of the folding of protein structural families we compare the effect of mutation in two closely related fibronectin type III (fnIII) domains, the tenth fnIII domain of human fibronectin (FNfn10) and the third fnIII domain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7ff7b015cceb013246ea7b7cc9f729e
https://pubmed.ncbi.nlm.nih.gov/10986129
https://pubmed.ncbi.nlm.nih.gov/10986129
Publikováno v:
Journal of molecular biology. 297(1)
TNfn3, the third fibronectin type III domain of human tenascin, is an immunoglobulin-like protein that is a good model for experimental and theoretical analyses of Greek key folding. The third fibronectin type III domain of human tenascin folds and u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7c5d3bdac0b02b95902651928d3e2fe
https://pubmed.ncbi.nlm.nih.gov/10704314
https://pubmed.ncbi.nlm.nih.gov/10704314
Publikováno v:
Structure (London, England : 1993). 7(9)
Background: Are folding pathways conserved in protein families? To test this explicitly and ask to what extent structure specifies folding pathways requires comparison of proteins with a common fold. Our strategy is to choose members of a highly dive
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::337c152276f05ff57f92d974099a0ff8
https://pubmed.ncbi.nlm.nih.gov/10508783
https://pubmed.ncbi.nlm.nih.gov/10508783
Autor:
Jane Clarke, Mark Bycroft, Stefan J. Hamill, Alex Bateman, Cyrus Chothia, Richard Sandford, Ruth Thomas
Publikováno v:
The EMBO journal. 18(2)
Most cases of autosomal dominant polycystic kidney disease (ADPKD) are the result of mutations in the PKD1 gene. The PKD1 gene codes for a large cell-surface glycoprotein, polycystin-1, of unknown function, which, based on its predicted domain struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eca60c850a647a70d6c51527db160697
https://pubmed.ncbi.nlm.nih.gov/9889186
https://pubmed.ncbi.nlm.nih.gov/9889186
Publikováno v:
Biochemistry. 37(22)
Correct selection of domain boundaries is critical for structural analysis of single domains from multimodular proteins. Folding and stability studies of the third fibronectin type III domain from human tenascin (TNfn31-90) have shown that it is mode
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e6faffb7a1daed743f1a5d1c532dd254
https://pubmed.ncbi.nlm.nih.gov/9609701
https://pubmed.ncbi.nlm.nih.gov/9609701
Autor:
Stefan M.V. Freund, Stefan J. Hamill, Guy M. Benian, Sun Fong, Mark R. Proctor, Mark Bycroft, Jane Clarke, Cyrus Chothia
Publikováno v:
Journal of molecular biology. 264(3)
The NMR solution structure of an immunoglobulin superfamily module of twitchin (Ig 18') has been determined and the kinetic and equilibrium folding behaviour characterised. Thirty molecular coordinates were calculated using a hybrid distance geometry
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::92d8781ac6ce16baef6cf2c6b1d2eac3
https://pubmed.ncbi.nlm.nih.gov/8969309
https://pubmed.ncbi.nlm.nih.gov/8969309