Estimation of free energy barriers in the cytoplasmic and mitochondrial aspartate aminotransferase reactions probed by hydrogen-exchange kinetics of C.alpha.-labeled amino acids with solvent

Biochemistry ◽  
1989 ◽  
Vol 28 (9) ◽  
pp. 3815-3821 ◽  
Author(s):  
Douglas A. Julin ◽  
Heinrich Wiesinger ◽  
Michael D. Toney ◽  
Jack F. Kirsch
Keyword(s):  
Amino Acids ◽  
Free Energy ◽  
Aspartate Aminotransferase ◽  
Hydrogen Exchange ◽  
Energy Barriers ◽  
Mitochondrial Aspartate Aminotransferase ◽  
Exchange Kinetics ◽  
Kinetics Of

scholarly journals Hydrogen exchange kinetics of human hemoglobins. The pH dependence of solvent accessibility in cyanomet-, oxy-, and deoxyhemoglobin.

1978 ◽  
Vol 253 (10) ◽  
pp. 3702-3707
Author(s):  
B.E. Hedlund ◽  
P.E. Hallaway ◽  
B.E. Hallaway ◽  
E.S. Benson ◽  
A. Rosenberg
Keyword(s):  
Hydrogen Exchange ◽  
Solvent Accessibility ◽  
Ph Dependence ◽  
Exchange Kinetics ◽  
Kinetics Of

Hydrogen exchange kinetics of core peptide protons in Streptomyces subtilisin inhibitor

Biochemistry ◽  
1985 ◽  
Vol 24 (12) ◽  
pp. 2973-2979 ◽  
Author(s):  
Kazuyuki Akasaka ◽  
Tomoko Inoue ◽  
Hiroyuki Hatano ◽  
Clare K. Woodward
Keyword(s):  
Hydrogen Exchange ◽  
Core Peptide ◽  
Exchange Kinetics ◽  
Subtilisin Inhibitor ◽  
Kinetics Of

Transcerebral exchange kinetics of large neutral amino acids during acute inspiratory hypoxia in humans

2019 ◽  
Vol 79 (8) ◽  
pp. 595-600
Author(s):  
Rasmus H. Dahl ◽  
Ronan M. G. Berg ◽  
Sarah Taudorf ◽  
Damian M. Bailey ◽  
Carsten Lundby ◽  
...  
Keyword(s):  
Amino Acids ◽  
Large Neutral Amino Acids ◽  
Neutral Amino Acids ◽  
Exchange Kinetics ◽  
Kinetics Of

Hydrogen-exchange kinetics of the indole NH proton of the buried tryptophan in the constant fragment of the immunoglobulin light chain

Biochemistry ◽  
1988 ◽  
Vol 27 (1) ◽  
pp. 346-350 ◽  
Author(s):  
Yasushi Kawata ◽  
Yuji Goto ◽  
Kozo Hamaguchi ◽  
Fumiaki Hayashi ◽  
Yuji Kobayashi ◽  
...  
Keyword(s):  
Light Chain ◽  
Hydrogen Exchange ◽  
Immunoglobulin Light Chain ◽  
Exchange Kinetics ◽  
Kinetics Of

Hydrogen Exchange Kinetics of RNase A and the Urea:TMAO Paradigm†

Biochemistry ◽  
2003 ◽  
Vol 42 (19) ◽  
pp. 5837-5849 ◽  
Author(s):  
Youxing Qu ◽  
D. Wayne Bolen
Keyword(s):  
Hydrogen Exchange ◽  
Rnase A ◽  
Exchange Kinetics ◽  
Kinetics Of

Macromolecular conformations and interactions

2018 ◽  
Author(s):  
Dennis Sherwood ◽  
Paul Dalby
Keyword(s):  
Amino Acids ◽  
Free Energy ◽  
Protein Folding ◽  
Energy Minimum ◽  
Huge Number ◽  
Thermodynamics And Kinetics ◽  
Ligand Interactions ◽  
Kinetics Of ◽  
Single Configuration ◽  
Over Time

As a polymer of many amino acids, any given protein can, in principle, adopt a huge number of configurations. In reality, however, the biologically stable protein adopts a single configuration that is stable over time. Thermodynamically, this configuration must represent a Gibbs free energy minimum. This chapter therefore explores how the thermodynamics and kinetics of protein folding and unfolding can be investigated experimentally (using, for example, chaotropes, heating or ligand interactions), and how these measurements can be used to enrich our understanding of protein configurations and stability.

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