Hydrogen-exchange study of lysozyme conformation changes induced by inhibitor binding

Biochemistry ◽  
1974 ◽  
Vol 13 (16) ◽  
pp. 3273-3277 ◽  
Author(s):  
R. R. Wickett ◽  
G. J. Ide ◽  
A. Rosenberg
Keyword(s):  
Hydrogen Exchange ◽  
Inhibitor Binding ◽  
Conformation Changes ◽  
Exchange Study

A Deuterium-Hydrogen Exchange Study of Inhibitor-Induced Conformational Changes in Ribonuclease A

1971 ◽  
Vol 21 (3) ◽  
pp. 393-399 ◽  
Author(s):  
Genevieve Nonnenmacher ◽  
Eliane Viala ◽  
Jean Marie Thiery ◽  
Paul Calvet
Keyword(s):  
Conformational Changes ◽  
Hydrogen Exchange ◽  
Ribonuclease A ◽  
Exchange Study

scholarly journals Hydrogen-exchange study of a nucleosome

FEBS Letters ◽  
1980 ◽  
Vol 121 (1) ◽  
pp. 130-132 ◽  
Author(s):  
Yuko Mitane ◽  
Mamoru Nakanishi ◽  
Tsuboi Masamichi ◽  
Kohwi-Shigematsu Terumi ◽  
Enomoto Takemi ◽  
...  
Keyword(s):  
Hydrogen Exchange ◽  
Exchange Study

scholarly journals A hydrogen exchange study of Escherichia coli 5S RNA

1981 ◽  
Vol 9 (16) ◽  
pp. 4081-4086 ◽  
Author(s):  
J. Ramstein ◽  
V.A. Erdmann
Keyword(s):  
Escherichia Coli ◽  
Hydrogen Exchange ◽  
5S Rna ◽  
Exchange Study

scholarly journals Deviation from the Residue-Based Linear Free Energy Relationship Reveals a Non-Native Structure in Protein Folding

2022 ◽  
Author(s):  
Daisuke Fujinami ◽  
Seiichiro Hayashi ◽  
Daisuke Kohda
Keyword(s):  
Free Energy ◽  
Protein Folding ◽  
Linear Relationship ◽  
Hydrogen Exchange ◽  
Structural Changes ◽  
Linear Free Energy Relationship ◽  
Native Structure ◽  
Linear Free Energy ◽  
Exchange Study ◽  
Protein Molecules

Multiprobe measurements, such as NMR and hydrogen exchange study, can provide the equilibrium constant K and kinetic rate constant k of the structural changes of a polypeptide on a per-residue basis. We previously found a linear relationship between residue-specific log K values and residue-specific log k values for the two-state topological isomerization of a 27-residue peptide. To test the general applicability of the residue-based linear free energy relationship (rbLEFR), we performed a literature search to collect residue-specific equilibrium and kinetic constants in various exchange processes, including protein folding, coupled folding and binding of intrinsically disordered peptides, and structural fluctuations of folded proteins. The good linearity in a substantial number of log-log plots proved that the rbLFER holds for the structural changes in a wide variety of protein-related phenomena. Protein molecules quickly fold into their native structures and change their conformations smoothly. Theoretical studies and molecular simulations advocate that the physicochemical basis is the consistency principle and the minimal frustration principle: Non-native structures/interactions are absent or minimized along the folding pathway. The linearity of the residue-based free energy relationship demonstrates experimentally the absence of non-native structures in transition states. In this context, the hydrogen exchange study of apomyoglobin folding intermediates is particularly interesting. We found that the residues that deviated from the linear relationship corresponded to the non-native structure, which had been identified by other experiments. The rbLFER provides a unique and practical method to probe the dynamic aspects of the transition states of protein molecules.

Asymmetric opening reaction mechanism of Z-DNA base pairs: a hydrogen exchange study

Biochemistry ◽  
1985 ◽  
Vol 24 (14) ◽  
pp. 3603-3609 ◽  
Author(s):  
Jean Ramstein ◽  
Nicolas Vogt ◽  
Marc Leng
Keyword(s):  
Reaction Mechanism ◽  
Hydrogen Exchange ◽  
Base Pairs ◽  
Exchange Study ◽  
Dna Base ◽  
Dna Base Pairs ◽  
Z Dna
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