Zobrazeno 1 - 10
of 137
pro vyhledávání: '"Frederic M. Richards"'
Publikováno v:
Journal of Molecular Biology. 299:487-498
We have used the occluded surface algorithm to estimate the packing of both buried and exposed amino acid residues in protein structures. This method works equally well for buried residues and solvent-exposed residues in contrast to the commonly used
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::389cb8231b60eb3361a07974787fe16e
https://doi.org/10.1006/jmbi.2000.3750
https://doi.org/10.1006/jmbi.2000.3750
Publikováno v:
Protein Science. 9:2506-2517
Methylene is one of, if not the, most reactive organic chemical known. It has a very low specificity, which makes it essentially useless for synthesis, but suggests a possible role in protein footprinting with special importance in labeling solvent a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cf8ec80f297bde924c615f928acd6e6
https://doi.org/10.1110/ps.9.12.2506
https://doi.org/10.1110/ps.9.12.2506
Autor:
Frederic M. Richards
Publikováno v:
Annual Review of Biophysics and Biomolecular Structure. 26:1-25
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d14885f6b2b9d76b49a80fc00ffd1063
https://doi.org/10.1146/annurev.biophys.26.1.1
https://doi.org/10.1146/annurev.biophys.26.1.1
Publikováno v:
Protein Science. 5:1026-1031
The structures of several variants of staphylococcal nuclease with long flexible unnatural amino acid side chains in the hydrophobic core have been determined by X-ray crystallography. The unnatural amino acids are disulfide moieties between the lone
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1cd86e266543f88b5fa6a201b06a9fa7
https://doi.org/10.1002/pro.5560050605
https://doi.org/10.1002/pro.5560050605
Publikováno v:
Biochemistry. 34:11807-11813
The reduction of disulfides by thioredoxin involves a two-step mechanism. The first step features an intermolecular attack of Cys32 of thioredoxin on the disulfide with formation of a protein mixed disulfide and release of 1 equiv of thiol. The secon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5619b4331b694f758a67b9765af8576
https://doi.org/10.1021/bi00037a019
https://doi.org/10.1021/bi00037a019
Publikováno v:
Nature. 372:375-379
The Src-homology-3 (SH3) domains of the Caenorhabditis elegans protein SEM-5 and its human and Drosophila homologues, Grb2 and Drk (refs 1-4), bind proline-rich sequences found in the nucleotide-exchange factor Sos as part of their proposed function
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27c990483ef234d452d7024b10e8a842
https://doi.org/10.1038/372375a0
https://doi.org/10.1038/372375a0
Autor:
Julian M. Sturtevant, Thomson Jg, Girish S. Ratnaparkhi, Raghavan Varadarajan, Frederic M. Richards
Publikováno v:
Biochemistry. 33:8587-8593
Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex. We have substituted the wild-type residue at position 13, methionine (Met),
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::58e896c3d86947455a2879d137fb26c5
https://doi.org/10.1021/bi00194a025
https://doi.org/10.1021/bi00194a025
Autor:
Wendell A. Lim, Frederic M. Richards
Publikováno v:
Nature Structural & Molecular Biology. 1:221-225
Src homology 3 (SH3) domains bind specific proline-rich peptide motifs. To identify interactions involved in peptide recognition, we have mutated residues on the putative binding surface of an SH3 domain from the Caenorhabditis elegans protein Sem-5.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3858bf6bf5fef9aea6619c7037458a18
https://doi.org/10.1038/nsb0494-221
https://doi.org/10.1038/nsb0494-221
Autor:
Frederic M. Richards, Richard Wynn
Publikováno v:
Biochemistry. 32:12922-12927
Previously, we have introduced a method whereby novel disulfide side chains can be produced in the interior of a protein by modifying a cysteine residue after denaturant-induced unfolding [Wynn, R., & Richards, F. M. (1993) Proteins: Struct., Funct.,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b7f7f93fed18320936fe9c4206864e3f
https://doi.org/10.1021/bi00210a046
https://doi.org/10.1021/bi00210a046
Autor:
Frederic M. Richards, Wendell A. Lim
Publikováno v:
Quarterly Reviews of Biophysics. 26:423-498
The number of globular proteins for which high resolution structures are available is rapidly increasing. In each case the particular sequence of the polypeptide appears to yield only a single, compact, biologically active structure. However, peptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::93b7c951ff43d289afde263a5640de1d
https://doi.org/10.1017/s0033583500002845
https://doi.org/10.1017/s0033583500002845