scholarly journals Protein structural dynamics in solution unveiled via 100-ps time-resolved x-ray scattering

2010 ◽  
Vol 107 (16) ◽  
pp. 7281-7286 ◽  
Author(s):  
H. S. Cho ◽  
N. Dashdorj ◽  
F. Schotte ◽  
T. Graber ◽  
R. Henning ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Protein Structural Dynamics ◽  
Ray Scattering

scholarly journals X-ray Scattering Studies of Protein Structural Dynamics

2017 ◽  
Vol 117 (12) ◽  
pp. 7615-7672 ◽  
Author(s):  
Steve P. Meisburger ◽  
William C. Thomas ◽  
Maxwell B. Watkins ◽  
Nozomi Ando
Keyword(s):  
Structural Dynamics ◽  
X Ray ◽  
X Ray Scattering ◽  
Protein Structural Dynamics ◽  
Ray Scattering

scholarly journals Revealing Fast Structural Dynamics in pH-Responsive Peptides with Time-Resolved X-ray Scattering

2019 ◽  
Vol 123 (9) ◽  
pp. 2016-2021 ◽  
Author(s):  
Dolev Rimmerman ◽  
Denis Leshchev ◽  
Darren J. Hsu ◽  
Jiyun Hong ◽  
Baxter Abraham ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Ph Responsive ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008 ◽  
Vol 5 (10) ◽  
pp. 881-886 ◽  
Author(s):  
Marco Cammarata ◽  
Matteo Levantino ◽  
Friedrich Schotte ◽  
Philip A Anfinrud ◽  
Friederike Ewald ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Wide Angle ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

scholarly journals Insulin hexamer dissociation dynamics revealed by photoinduced T-jumps and time-resolved X-ray solution scattering

2018 ◽  
Vol 17 (7) ◽  
pp. 874-882 ◽  
Author(s):  
Dolev Rimmerman ◽  
Denis Leshchev ◽  
Darren J. Hsu ◽  
Jiyun Hong ◽  
Baxter Abraham ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Temperature Jump ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Dissociation Dynamics ◽  
Ray Scattering

The structural dynamics of insulin hexamer dissociation were studied by the photoinduced temperature jump technique and monitored by time-resolved X-ray scattering.

scholarly journals Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers

2014 ◽  
Vol 369 (1647) ◽  
pp. 20130318 ◽  
Author(s):  
Richard Neutze
Keyword(s):  
Structural Dynamics ◽  
Free Electron ◽  
Free Electron Lasers ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Protein Structural Dynamics ◽  
Structural Biochemistry ◽  
Scientific Questions ◽  
Serial Femtosecond Crystallography

X-ray free-electron lasers (XFELs) are revolutionary X-ray sources. Their time structure, providing X-ray pulses of a few tens of femtoseconds in duration; and their extreme peak brilliance, delivering approximately 10 12 X-ray photons per pulse and facilitating sub-micrometre focusing, distinguish XFEL sources from synchrotron radiation. In this opinion piece, I argue that these properties of XFEL radiation will facilitate new discoveries in life science. I reason that time-resolved serial femtosecond crystallography and time-resolved wide angle X-ray scattering are promising areas of scientific investigation that will be advanced by XFEL capabilities, allowing new scientific questions to be addressed that are not accessible using established methods at storage ring facilities. These questions include visualizing ultrafast protein structural dynamics on the femtosecond to picosecond time-scale, as well as time-resolved diffraction studies of non-cyclic reactions. I argue that these emerging opportunities will stimulate a renaissance of interest in time-resolved structural biochemistry.

scholarly journals Erratum: Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008 ◽  
Vol 5 (11) ◽  
pp. 988-988 ◽  
Author(s):  
Marco Cammarata ◽  
Matteo Levantino ◽  
Friedrich Schotte ◽  
Philip A Anfinrud ◽  
Friederike Ewald ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Wide Angle ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
Ray Scattering

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.

Time-Resolved Cryo-Electron Microscopy of Oscillating Microtubules

1990 ◽  
Vol 48 (1) ◽  
pp. 502-503
Author(s):  
Eva-Maria Mandelkow ◽  
Ron Milligan
Keyword(s):  
Electron Microscopy ◽  
Dynamic Instability ◽  
Entire Solution ◽  
Reaction Scheme ◽  
Time Resolved ◽  
X Ray ◽  
X Ray Scattering ◽  
A Chain ◽  
Ray Scattering

Microtubules form part of the cytoskeleton of eukaryotic cells. They are hollow libers of about 25 nm diameter made up of 13 protofilaments, each of which consists of a chain of heterodimers of α-and β-tubulin. Microtubules can be assembled in vitro at 37°C in the presence of GTP which is hydrolyzed during the reaction, and they are disassembled at 4°C. In contrast to most other polymers microtubules show the behavior of “dynamic instability”, i.e. they can switch between phases of growth and phases of shrinkage, even at an overall steady state [1]. In certain conditions an entire solution can be synchronized, leading to autonomous oscillations in the degree of assembly which can be observed by X-ray scattering (Fig. 1), light scattering, or electron microscopy [2-5]. In addition such solutions are capable of generating spontaneous spatial patterns [6].In an earlier study we have analyzed the structure of microtubules and their cold-induced disassembly by cryo-EM [7]. One result was that disassembly takes place by loss of protofilament fragments (tubulin oligomers) which fray apart at the microtubule ends. We also looked at microtubule oscillations by time-resolved X-ray scattering and proposed a reaction scheme [4] which involves a cyclic interconversion of tubulin, microtubules, and oligomers (Fig. 2). The present study was undertaken to answer two questions: (a) What is the nature of the oscillations as seen by time-resolved cryo-EM? (b) Do microtubules disassemble by fraying protofilament fragments during oscillations at 37°C?

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