scholarly journals Monitoring Aromatic Picosecond to Nanosecond Dynamics in Proteins via13C Relaxation: Expanding Perturbation Mapping of the Rigidifying Core Mutation, V54A, in Eglin c†

Biochemistry ◽  
2008 ◽  
Vol 47 (17) ◽  
pp. 4876-4886 ◽  
Author(s):  
Joshua A. Boyer ◽  
Andrew L. Lee
Keyword(s):  
Eglin C ◽  
Nanosecond Dynamics

Crystal and molecular structure of the bovine α-chymotrypsin-eglin c complex at 2.0 Å resolution

1992 ◽  
Vol 225 (1) ◽  
pp. 107-123 ◽  
Author(s):  
Francesco Frigerio ◽  
Alessandro Coda ◽  
Luisa Pugliese ◽  
Claudia Lionetti ◽  
Enea Menegatti ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Crystal And Molecular Structure ◽  
Eglin C ◽  
C Complex

Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c

1989 ◽  
Vol 45 (5) ◽  
pp. 488-499 ◽  
Author(s):  
P. Gros ◽  
M. Fujinaga ◽  
B. W. Dijkstra ◽  
K. H. Kalk ◽  
W. G. J. Hol
Keyword(s):  
Molecular Dynamics ◽  
Serine Protease ◽  
Eglin C

Influence of cosolvents, self-crowding, temperature and pressure on the sub-nanosecond dynamics and folding stability of lysozyme

2017 ◽  
Vol 19 (22) ◽  
pp. 14230-14237 ◽  
Author(s):  
S. R. Al-Ayoubi ◽  
P. H. Schummel ◽  
M. Golub ◽  
J. Peters ◽  
R. Winter
Keyword(s):  
Hydrostatic Pressure ◽  
Temperature And Pressure ◽  
Nanosecond Dynamics

Self-crowding and osmolytes are able to affect the fast dynamics of proteins more efficiently than hydrostatic pressure.

scholarly journals Nanosecond Dynamics of Calmodulin and Ribosome-Bound Nascent Chains Studied by Time-Resolved Fluorescence Anisotropy

2014 ◽  
Vol 106 (2) ◽  
pp. 670a-671a
Author(s):  
Daryan Kempe ◽  
Paraskevas Lamprou ◽  
Alexandros Katranidis ◽  
Georg Büldt ◽  
Jörg Fitter
Keyword(s):  
Fluorescence Anisotropy ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Nanosecond Dynamics

Complex between the subtilisin from a mesophilic bacterium and the Leech inhibitor eglin-C

1991 ◽  
Vol 47 (5) ◽  
pp. 707-730 ◽  
Author(s):  
Z. Dauter ◽  
C. Betzel ◽  
N. Genov ◽  
N. Pipon ◽  
K. S. Wilson
Keyword(s):  
Eglin C ◽  
Mesophilic Bacterium

Changing the inhibitory specificity and function of the proteinase inhibitor eglin c by site-directed mutagenesis: functional and structural investigation

Biochemistry ◽  
1992 ◽  
Vol 31 (37) ◽  
pp. 8755-8766 ◽  
Author(s):  
Dirk W. Heinz ◽  
Sven G. Hyberts ◽  
Jeff W. Peng ◽  
John P. Priestle ◽  
Gerhard Wagner ◽  
...  
Keyword(s):  
Proteinase Inhibitor ◽  
Structural Investigation ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Inhibitory Specificity ◽  
Eglin C ◽  
And Function

Effect of a Polyhistidine Terminal Extension on Eglin c Stability

1998 ◽  
Vol 263 (1) ◽  
pp. 116-118 ◽  
Author(s):  
Jennifer C. Waldner ◽  
Steven J. Lahr ◽  
Marshall Hall Edgell ◽  
Gary J. Pielak
Keyword(s):  
Eglin C

Protease Inhibitor Eglin-C Affects Superoxide Anion Release but not Bacterial Killing by Human Polymorphonuclear Leukocytes

1988 ◽  
Vol 14 (6) ◽  
pp. 743-756 ◽  
Author(s):  
Anthony L. Esposito ◽  
Carolyn A. Clark ◽  
William J. Poirier ◽  
Phyllis A. Kephart
Keyword(s):  
Protease Inhibitor ◽  
Superoxide Anion ◽  
Polymorphonuclear Leukocytes ◽  
Bacterial Killing ◽  
Eglin C ◽  
Human Polymorphonuclear Leukocytes

ICAM-1-CD18 interaction mediates neutrophil cytotoxicity through protease release

1998 ◽  
Vol 274 (6) ◽  
pp. C1634-C1644 ◽  
Author(s):  
Carlton C. Barnett ◽  
Ernest E. Moore ◽  
Gary W. Mierau ◽  
David A. Partrick ◽  
Walter L. Biffl ◽  
...  
Keyword(s):  
Cho Cells ◽  
Chinese Hamster ◽  
Cell Lysis ◽  
Polymorphonuclear Neutrophil ◽  
Intercellular Adhesion Molecule ◽  
Wild Type ◽  
Myristate Acetate ◽  
Intercellular Adhesion Molecule 1 ◽  
Eglin C

Interaction of the β2-integrin complex on the polymorphonuclear neutrophil (PMN) with intercellular adhesion molecule-1 (ICAM-1) has been implicated in PMN-mediated cytotoxicity. This study examined interaction of the CD11a, CD11b, and CD18 subunits of the β2-integrin with ICAM-1, transfected into Chinese hamster ovarian (CHO) cells to avoid effects of other adhesion molecules. Incubation of quiescent PMNs with wild-type and ICAM-1-transfected CHO cells produced nominal cell lysis. Similarly, when phorbol myristate acetate (PMA)-activated PMNs were incubated with wild-type CHO cells, minimal cytotoxicity was produced. However, when ICAM-1-transfected CHO cells were incubated with PMA-activated PMNs, 40% cell lysis occurred. Blockade with a monoclonal antibody (MAb) to ICAM-1 or MAbs to CD11a, CD11b, or CD18 reduced PMN-mediated cytotoxicity to baseline. To examine the role of adhesion in cytotoxicity, we studied β2-integrin-mediated PMN adhesion to ICAM-1-transfected CHO cells and found that MAbs for CD11a, CD11b, and CD18 all abrogated PMN cytotoxicity despite disparate effects on adhesion. To assess the role of CD18, β2-integrin subunits were cross-linked, and CD18 alone mediated protease release. Moreover, ICAM-1 was immunoprecipitated from transfected CHO cells and incubated with PMNs. This soluble ICAM-1 provoked elastase release, similar to PMA, which could be inhibited by MAbs to CD18 but not MAbs to other β2-integrin subunits. In addition, coincubation with protease inhibitors eglin C and AAPVCK reduced PMN-mediated cytotoxicity to control levels. Finally, ICAM-1-transfected CHO cells were exposed to activated PMNs from a patient with chronic granulomatous disease that caused significant cell lysis, equivalent to that of PMNs from normal donors. Collectively, these data suggest that ICAM-1 provokes PMN-mediated cytotoxicity via CD18-mediated protease release.

Nanosecond dynamics of horse heart apocytochrome c in aqueous solution as studied by time-resolved fluorescence of the single tryptophan residue (Trp-59)

Biochemistry ◽  
1988 ◽  
Vol 27 (24) ◽  
pp. 8752-8761 ◽  
Author(s):  
Michel Vincent ◽  
Jean Claude Brochon ◽  
Fabienne Merola ◽  
Wilco Jordi ◽  
Jacques Gallay
Keyword(s):  
Aqueous Solution ◽  
Tryptophan Residue ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Apocytochrome C ◽  
Nanosecond Dynamics
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