Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Douglas A. Simmons"'
Autor:
Carol V. Robinson, Brandon T. Ruotolo, Justin L. P. Benesch, Nina Morgner, Helen R. Saibil, Douglas A. Simmons, Nelson P. Barrera, Luchun Wang
Publikováno v:
Journal of Structural Biology; Vol 172
Journal of Structural Biology
Journal of Structural Biology
Many multi-protein assemblies exhibit characteristics which hamper their structural and dynamical characterization. These impediments include low copy number, heterogeneity, polydispersity, hydrophobicity, and intrinsic disorder. It is becoming incre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb759925eb084a03a39b18c10f58af66
https://ora.ox.ac.uk/objects/uuid:9e96bd53-c7c4-429c-82d5-7a03fa59bf43
https://ora.ox.ac.uk/objects/uuid:9e96bd53-c7c4-429c-82d5-7a03fa59bf43
Autor:
Robert H. H. van den Heuvel, Harm van Heerikhuizen, Douglas A. Simmons, Patrick J. Bakkes, Albert J. R. Heck, Ron M. A. Heeren, Carol V. Robinson, Esther van Duijn, Saskia M. van der Vies
It has been suggested that the bacterial GroEL chaperonin accommodates only one substrate at any given time, due to conformational changes to both the cis and trans ring that are induced upon substrate binding. Using electrospray ionization mass spec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c870fb988ff496aaac991748dd4349c
https://ora.ox.ac.uk/objects/uuid:8ddc141b-229c-4f90-ab0c-6d87ce0e8407
https://ora.ox.ac.uk/objects/uuid:8ddc141b-229c-4f90-ab0c-6d87ce0e8407
Publikováno v:
Canadian Journal of Chemistry. 83:1953-1960
Electrospray ionization (ESI) mass spectrometry (MS) has become a popular tool for monitoring ligandprotein and proteinprotein interactions. Due to the "gentle" nature of the ionization process, it is often possible to transfer weakly bound compl
Autor:
Douglas A. Simmons, Lars Konermann
Publikováno v:
Mass Spectrometry Reviews. 22:1-26
The "protein-folding problem" refers to the question of how and why a denatured polypeptide chain can spontaneously fold into a compact and highly ordered conformation. The classical description of this process in terms of reaction pathways has been
Autor:
Douglas A. Simmons, Lars Konermann
Publikováno v:
Biochemistry. 41:1906-1914
A novel technique for studying protein folding kinetics is presented. It is based on a continuous-flow setup that is coupled to an electrospray (ESI) mass spectrometer and allows initiation of a folding reaction, followed by isotopic pulse labeling.
Publikováno v:
Rapid Communications in Mass Spectrometry. 14:772-776
In this work a new mass spectrometry based method for monitoring the kinetics of chemical reactions in solution is described. A stopped-flow mixing instrument is coupled to an electrospray ionization (ESI) mass spectrometer via a novel type of interf
Publikováno v:
Journal of the American Society for Mass Spectrometry. 11:312-319
In most cases, kinetic unfolding reactions of proteins follow a simple one-step mechanism that does not involve any detectable intermediates. One example for a more complicated unfolding reaction is the acid-induced denaturation of holo-myoglobin (hM
Publikováno v:
Chemical reviews. 107(8)
A review on the application of mass spectrometry (MS) to the upper levels of protein organization is presented. A description on the processes of generating, transmitting, and analyzing ions formed by protein complexes is presented as well as the exp
Publikováno v:
Expert review of proteomics. 2(4)
One of the greatest current challenges in proteomics is to develop an understanding of cellular communication and regulation processes, most of which involve noncovalent interactions of proteins with various binding partners. Mass spectrometry plays
Publikováno v:
Texas dental journal. 122(3)