Ligand Dissociation Process from Myoglobin Monitored by the Time-Resolved Volume Change

2006 ◽  
Vol 53 (1) ◽  
pp. 253-262 ◽  
Author(s):  
Masahide Terazima
Keyword(s):  
Volume Change ◽  
Dissociation Process ◽  
Time Resolved ◽  
Ligand Dissociation

scholarly journals Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase

2009 ◽  
Vol 11 (3) ◽  
pp. 558-570 ◽  
Author(s):  
Keehwan Kwon ◽  
Emily D. Streaker ◽  
Dorothy Beckett
Keyword(s):  
Binding Specificity ◽  
Dissociation Process ◽  
E Coli ◽  
Ligand Dissociation

scholarly journals Capturing Functionally Relevant Protein Motions at the Atomic Level: Femtosecond Time Resolved Serial Crystallography of Ligand Dissociation of Carboxy-Myoglobin

2016 ◽  
Vol 110 (3) ◽  
pp. 513a ◽  
Author(s):  
Henrike M. Müller-Werkmeister ◽  
Anling Kuo ◽  
Helen M. Ginn ◽  
Saeed Oghbaey ◽  
Antoine Sarracini ◽  
...  
Keyword(s):  
Atomic Level ◽  
Time Resolved ◽  
Ligand Dissociation ◽  
Protein Motions ◽  
Serial Crystallography

Protein dynamics detected by the time-resolved transient grating technique

2001 ◽  
Vol 73 (3) ◽  
pp. 513-517
Author(s):  
Masahide Terazima
Keyword(s):  
Protein Dynamics ◽  
Volume Change ◽  
Transient Absorption ◽  
Photoactive Yellow Protein ◽  
Absorption Method ◽  
Transient Grating ◽  
Time Resolved ◽  
Acoustic Methods ◽  
Temporal Profiles

Dynamics of two proteins [myoglobin and photoactive yellow protein (PYP)] initiated by photoexcitation were studied by the time-resolved transient grating (TG) and photo-acoustic methods. For both proteins, the temporal profiles of the TG signals showed new features that have not been detected before by the transient absorption method. These dynamics were attributed to the volume change, which is caused by the protein dynamics apart from the chromophores.

Stereomutation at hexacoordinate silicon by a ligand-dissociation process

1984 ◽  
Vol 106 (14) ◽  
pp. 3992-3994 ◽  
Author(s):  
William B. Farnham ◽  
John F. Whitney
Keyword(s):  
Dissociation Process ◽  
Ligand Dissociation

Microtubule nucleation sequence studied by time-resolved x-ray scattering and electron microscopy

1983 ◽  
Vol 41 ◽  
pp. 766-767
Author(s):  
Eva-Maria Mandelkow ◽  
Eckhard Mandelkow ◽  
Joan Bordas
Keyword(s):  
Electron Microscopy ◽  
Dynamic Equilibrium ◽  
Time Resolved ◽  
X Ray ◽  
Additional Information ◽  
X Ray Scattering ◽  
Low Concentrations ◽  
Microtubule Growth ◽  
Ray Patterns ◽  
Ray Scattering

When a solution of microtubule protein is changed from non-polymerising to polymerising conditions (e.g. by temperature jump or mixing with GTP) there is a series of structural transitions preceding microtubule growth. These have been detected by time-resolved X-ray scattering using synchrotron radiation, and they may be classified into pre-nucleation and nucleation events. X-ray patterns are good indicators for the average behavior of the particles in solution, but they are difficult to interpret unless additional information on their structure is available. We therefore studied the assembly process by electron microscopy under conditions approaching those of the X-ray experiment. There are two difficulties in the EM approach: One is that the particles important for assembly are usually small and not very regular and therefore tend to be overlooked. Secondly EM specimens require low concentrations which favor disassembly of the particles one wants to observe since there is a dynamic equilibrium between polymers and subunits.

Electron Channeling Patterns

1977 ◽  
Vol 35 ◽  
pp. 12-13
Author(s):  
David C. Joy
Keyword(s):  
Electron Diffraction ◽  
Incidence Angle ◽  
Photographic Plate ◽  
Diffraction Effect ◽  
Angle Of Incidence ◽  
Bulk Single Crystal ◽  
Time Resolved ◽  
Electron Channeling ◽  
Spatially Resolved ◽  
Large Bulk

Electron channeling patterns (ECP) were first found by Coates (1967) while observing a large bulk, single crystal of silicon in a scanning electron microscope. The geometric pattern visible was shown to be produced as a result of the changes in the angle of incidence, between the beam and the specimen surface normal, which occur when the sample is examined at low magnification (Booker, Shaw, Whelan and Hirsch 1967).A conventional electron diffraction pattern consists of an angularly resolved intensity distribution in space which may be directly viewed on a fluorescent screen or recorded on a photographic plate. An ECP, on the other hand, is produced as the result of changes in the signal collected by a suitable electron detector as the incidence angle is varied. If an integrating detector is used, or if the beam traverses the surface at a fixed angle, then no channeling contrast will be observed. The ECP is thus a time resolved electron diffraction effect. It can therefore be related to spatially resolved diffraction phenomena by an application of the concepts of reciprocity (Cowley 1969).

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