scholarly journals Direct Observation of Cooperative Protein Structural Dynamics of Homodimeric Hemoglobin from 100 ps to 10 ms with Pump–Probe X-ray Solution Scattering

2012 ◽  
Vol 134 (16) ◽  
pp. 7001-7008 ◽  
Author(s):  
Kyung Hwan Kim ◽  
Srinivasan Muniyappan ◽  
Key Young Oang ◽  
Jong Goo Kim ◽  
Shunsuke Nozawa ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Direct Observation ◽  
Pump Probe ◽  
X Ray ◽  
Protein Structural Dynamics

Protein Structural Dynamics of Photoactive Yellow Protein in Solution Revealed by Pump–Probe X-ray Solution Scattering

2012 ◽  
Vol 134 (6) ◽  
pp. 3145-3153 ◽  
Author(s):  
Tae Wu Kim ◽  
Jae Hyuk Lee ◽  
Jungkweon Choi ◽  
Kyung Hwan Kim ◽  
Luuk J. van Wilderen ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Photoactive Yellow Protein ◽  
Pump Probe ◽  
X Ray ◽  
Protein Structural Dynamics

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 Direct observation of myoglobin structural dynamics from 100 picoseconds to 1 microsecond with picosecond X-ray solution scattering

2011 ◽  
Vol 47 (1) ◽  
pp. 289-291 ◽  
Author(s):  
Kyung Hwan Kim ◽  
Key Young Oang ◽  
Jeongho Kim ◽  
Jae Hyuk Lee ◽  
Youngmin Kim ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Direct Observation ◽  
X Ray

Temperature-dependent X-ray diffraction as a probe of protein structural dynamics

Nature ◽  
1979 ◽  
Vol 280 (5723) ◽  
pp. 558-563 ◽  
Author(s):  
Hans Frauenfelder ◽  
Gregory A. Petsko ◽  
Demetrius Tsernoglou
Keyword(s):  
Structural Dynamics ◽  
X Ray Diffraction ◽  
Temperature Dependent ◽  
X Ray ◽  
Protein Structural Dynamics

scholarly journals Cooperative protein structural dynamics of homodimeric hemoglobin linked to water cluster at subunit interface revealed by time-resolved X-ray solution scattering

2016 ◽  
Vol 3 (2) ◽  
pp. 023610 ◽  
Author(s):  
Jong Goo Kim ◽  
Srinivasan Muniyappan ◽  
Key Young Oang ◽  
Tae Wu Kim ◽  
Cheolhee Yang ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Water Cluster ◽  
Time Resolved ◽  
X Ray ◽  
Subunit Interface ◽  
Protein Structural Dynamics

scholarly journals Protein Structural Dynamics Revealed by Time-Resolved X-ray Solution Scattering

2015 ◽  
Vol 48 (8) ◽  
pp. 2200-2208 ◽  
Author(s):  
Jong Goo Kim ◽  
Tae Wu Kim ◽  
Jeongho Kim ◽  
Hyotcherl Ihee
Keyword(s):  
Structural Dynamics ◽  
Time Resolved ◽  
X Ray ◽  
Protein Structural Dynamics

scholarly journals Protein Structural Dynamics of Wild-Type and Mutant Homodimeric Hemoglobin Studied by Time-Resolved X-Ray Solution Scattering

2018 ◽  
Vol 19 (11) ◽  
pp. 3633 ◽  
Author(s):  
Cheolhee Yang ◽  
Minseo Choi ◽  
Jong Kim ◽  
Hanui Kim ◽  
Srinivasan Muniyappan ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Conformational Changes ◽  
Structural Transition ◽  
Quaternary Structure ◽  
Heme Binding ◽  
Wild Type ◽  
Time Resolved ◽  
X Ray ◽  
Protein Structural Dynamics ◽  
Cooperative Transition

The quaternary transition between the relaxed (R) and tense (T) states of heme-binding proteins is a textbook example for the allosteric structural transition. Homodimeric hemoglobin (HbI) from Scapharca inaequivalvis is a useful model system for investigating the allosteric behavior because of the relatively simple quaternary structure. To understand the cooperative transition of HbI, wild-type and mutants of HbI have been studied by using time-resolved X-ray solution scattering (TRXSS), which is sensitive to the conformational changes. Herein, we review the structural dynamics of HbI investigated by TRXSS and compare the results of TRXSS with those of other techniques.

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 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.

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