Hydrogen exchange kinetics in a membrane protein determined by nitrogen-15 NMR spectroscopy: use of the INEPT experiment to follow individual amides in detergent-solubilized M13 coat protein

Biochemistry ◽  
1990 ◽  
Vol 29 (26) ◽  
pp. 6303-6313 ◽  
Author(s):  
Gillian D. Henry ◽  
Brian D. Sykes
Keyword(s):  
Nmr Spectroscopy ◽  
Coat Protein ◽  
Membrane Protein ◽  
Hydrogen Exchange ◽  
Exchange Kinetics

Structure and dynamics of detergent-solubilized M13 coat protein (an integral membrane protein) determined by 13C and 15N nuclear magnetic resonance spectroscopy

1990 ◽  
Vol 68 (1) ◽  
pp. 318-329 ◽  
Author(s):  
Gillian D. Henry ◽  
Brian D. Sykes
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Coat Protein ◽  
Magnetic Resonance Spectroscopy ◽  
Membrane Protein ◽  
Nuclear Magnetic Resonance Spectroscopy ◽  
Hydrogen Exchange ◽  
Resonance Spectroscopy ◽  
Structure And Dynamics ◽  
Exchange Kinetics

The major coat protein of the filamentous bacteriophage M13 is inserted as an integral protein in the inner membrane of the Escherichia coli host upon infection. M13 coat protein is an ideal model membrane protein and has been the target of many biophysical studies. An overview is presented here of the application of nuclear magnetic resonance spectroscopy to the study of the structure and dynamics of M13 coat protein in several lipid-mimetic environments. The coat protein may be biosynthetically enriched with 13C- and 15N-labelled amino acids, allowing the resolution and assignment of individual nuclei. Structural fluctuations at selected sites have been monitored using 13C relaxation and isotope-detected amide hydrogen exchange kinetics. A model is proposed for the structure of a coat protein dimer in detergent micelles.Key words: protein dynamics, hydrogen-exchange kinetics, membrane protein, 13C- and 15N-NMR, isotope labels.

scholarly journals Base-Pair Opening Dynamics Study of Fluoride Riboswitch in the Bacillus cereus CrcB Gene

2021 ◽  
Vol 22 (6) ◽  
pp. 3234
Author(s):  
Juhyun Lee ◽  
Si-Eun Sung ◽  
Janghyun Lee ◽  
Jin Young Kang ◽  
Joon-Hwa Lee ◽  
...  
Keyword(s):  
Gene Expression ◽  
Gene Regulation ◽  
Nmr Spectroscopy ◽  
Bacillus Cereus ◽  
Base Pair ◽  
Noncoding Rna ◽  
Hydrogen Exchange ◽  
Magnesium Ion ◽  
Fluoride Ion ◽  
Base Pair Opening

Riboswitches are segments of noncoding RNA that bind with metabolites, resulting in a change in gene expression. To understand the molecular mechanism of gene regulation in a fluoride riboswitch, a base-pair opening dynamics study was performed with and without ligands using the Bacillus cereus fluoride riboswitch. We demonstrate that the structural stability of the fluoride riboswitch is caused by two steps depending on ligands. Upon binding of a magnesium ion, significant changes in a conformation of the riboswitch occur, resulting in the greatest increase in their stability and changes in dynamics by a fluoride ion. Examining hydrogen exchange dynamics through NMR spectroscopy, we reveal that the stabilization of the U45·A37 base-pair due to the binding of the fluoride ion, by changing the dynamics while maintaining the structure, results in transcription regulation. Our results demonstrate that the opening dynamics and stabilities of a fluoride riboswitch in different ion states are essential for the genetic switching mechanism.

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
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