Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Andrew F. Mehl"'
Publikováno v:
Biochemical and Biophysical Research Communications. 420:635-638
Insight into the stability and folding of oligomeric proteins is essential to the understanding of protein folding, especially since the majority of proteins found in nature are oligomeric. A deletion mutant of the GrpE protein from Escherichia coli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6ae845dab713fd96cb7c215fecb55b0
https://doi.org/10.1016/j.bbrc.2012.03.052
https://doi.org/10.1016/j.bbrc.2012.03.052
Publikováno v:
The Protein Journal. 26:239-245
The GrpE protein from E. coli is a homodimer with an unusual structure of two long paired alpha-helices from each monomer interacting in a parallel arrangement to form a "tail" at the N-terminal end. Using site-directed mutagenesis, we show that ther
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94c8295345780f29b02269f4acbdc4ed
https://doi.org/10.1007/s10930-006-9065-9
https://doi.org/10.1007/s10930-006-9065-9
Publikováno v:
Protein Science. 12:1205-1215
The GrpE heat shock protein from Escherichia coli has a homodimeric structure. The dimer interface encompasses two long alpha-helices at the NH(2)-terminal end from each monomer (forming a "tail"), which lead into a small four-helix bundle from which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::944a0272f2559dffcaf4e794f93b35fb
https://doi.org/10.1110/ps.0300803
https://doi.org/10.1110/ps.0300803
Publikováno v:
Biomacromolecules. 13(5)
A protein hydrogel system based on the assembly of a four-helix bundle motif was proposed and synthesized by genetic engineering methods. This new polypeptide, named GBH1, consists of identical amphipathic helices of 22 residues in length oriented in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f789092c39912ece65233578fc46682
https://pubmed.ncbi.nlm.nih.gov/22512688
https://pubmed.ncbi.nlm.nih.gov/22512688
Publikováno v:
Biochemistry. 33:1093-1102
The present study was carried out to determine the energetics of Clostridium symbiosum pyruvate phosphate dikinase (PPDK) catalyzed interconversion of adenosine 5'-triphosphate (ATP), orthophosphate (Pi), and pyruvate (pyr) with adenosine 5'-monophos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::54743f65a7987b16cbbc2119667f297a
https://doi.org/10.1021/bi00171a007
https://doi.org/10.1021/bi00171a007
Insight into protein stability and folding remains an important area for protein research, in particular protein-protein interactions and the self-assembly of homodimers. The GrpE protein from Escherichia coli is a homodimer with a four-helix bundle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::86459167cee096e78f891dd566b8b8eb
https://europepmc.org/articles/PMC3081660/
https://europepmc.org/articles/PMC3081660/
Publikováno v:
Biochemistry. 32:1803-1809
The intermediacy of a pyrophosphorylenzyme (E-PP) and phosphorylenzyme (E-P) in the Clostridium symbiosum pyruvate phosphate dikinase catalyzed interconversion of adenosine 5'-triphosphate (ATP), orthophosphate (Pi), and pyruvate with adenosine 5'-mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e705886fdd0b7b72e9a531e79207430c
https://doi.org/10.1021/bi00058a014
https://doi.org/10.1021/bi00058a014
Publikováno v:
Biochemical and biophysical research communications. 282(2)
A key feature to the dimeric structure for the GrpE heat shock protein is the pair of long helices at the NH,-terminal end followed by a presumable extended segment of about 30 amino acids from each monomer. We have constructed a GrpE deletion mutant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5edc4213da956b416ee2429dc8fcabaa
https://pubmed.ncbi.nlm.nih.gov/11401497
https://pubmed.ncbi.nlm.nih.gov/11401497
Publikováno v:
Biochemistry. 38(13)
Most, if not all, of the cellular functions of Hsp70 proteins require the assistance of a DnaJ homologue, which accelerates the weak intrinsic ATPase activity of Hsp70 and serves as a specificity factor by binding and targeting specific polypeptide s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b6888796f82dd1eb7681d5b12e694c5
https://pubmed.ncbi.nlm.nih.gov/10194333
https://pubmed.ncbi.nlm.nih.gov/10194333
Publikováno v:
Journal of Chemical Education. 86:600
Few laboratory procedures describe the use of circular dichroism (CD) at the undergraduate level. To increase the number of laboratory exercises using CD, a thermal denaturation study of myoglobin using CD is described to assess protein stability. Va
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a94df6266793096cb3e5e7145d9ac74
https://doi.org/10.1021/ed086p600
https://doi.org/10.1021/ed086p600