ArticleProceedings of the National Academy of Sciences of the United States of America2007
Disulfide bond influence on protein structural dynamics probed with 2D-IR vibrational echo spectroscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 67 citations in OpenAlex.
- Novel neutralizing SARS-CoV-2-specific mAbs offer detection of RBD linear epitopes.Virology journal · 2024Article
- Biomolecular infrared spectroscopy: making time for dynamics.Chemical science · 2024Review
- The influence of disulfide bonds on the mechanical stability of proteins is context dependent.The Journal of biological chemistry · 2017Article
- A primary role for disulfide formation in the productive folding of prokaryotic Cu,Zn-superoxide dismutase.The Journal of biological chemistry · 2014Article
- The effect of tensile stress on the conformational free energy landscape of disulfide bonds.PloS one · 2014Article
- pH-dependent picosecond structural dynamics in the distal pocket of nitrophorin 4 investigated by 2D IR spectroscopy.The journal of physical chemistry. B · 2013Article
- Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Topics in current chemistry · 2013Review
- Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
- Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand.The journal of physical chemistry. B · 2011Article
- Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water.The Journal of chemical physics · 2011Article
- Influence of histidine tag attachment on picosecond protein dynamics.Biochemistry · 2011Article
- Temperature dependent equilibrium native to unfolded protein dynamics and properties observed with IR absorption and 2D IR vibrational echo experiments.Journal of the American Chemical Society · 2011Article
- Protein dynamics in cytochrome P450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy.Journal of the American Chemical Society · 2011Article
- Neuroglobin and cytoglobin: two new members of globin family.Revista brasileira de hematologia e hemoterapia · 2011Article
- Conformational switching between protein substates studied with 2D IR vibrational echo spectroscopy and molecular dynamics simulations.The journal of physical chemistry. B · 2010Article
- Dynamics of a myoglobin mutant enzyme: 2D IR vibrational echo experiments and simulations.Journal of the American Chemical Society · 2010Article
- Characterization of azido-NAD+ to assess its potential as a two-dimensional infrared probe of enzyme dynamics.Analytical biochemistry · 2010Article
- Characterizing the dynamics of functionally relevant complexes of formate dehydrogenase.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Probing residue-specific interactions in the stabilization of proteins using high-resolution NMR: a study of disulfide bond compensation.Journal of pharmaceutical sciences · 2010Article
- Exploring the molecular origins of protein dynamics in the active site of human carbonic anhydrase II.The journal of physical chemistry. B · 2009Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Intramolecular disulfide bonds are understood to play a role in regulating protein stability and activity. Because disulfide bonds covalently link different components of a protein, they influence protein structure. However, the effects of disulfide bonds on fast (subpicosecond to approximately 100 ps) protein equilibrium structural fluctuations have not been characterized experimentally. Here, ultrafast 2D-IR vibrational echo spectroscopy is used to examine the constraints an intramolecular disulfide bond places on the structural fluctuations of the protein neuroglobin (Ngb). Ngb is a globin family protein found in vertebrate brains that binds oxygen reversibly. Like myoglobin (Mb), Ngb has the classical globin fold and key residues around the heme are conserved. Furthermore, the heme-ligated CO vibrational spectra of Mb (Mb-CO) and Ngb (Ngb-CO) are virtually identical. However, in contrast to Mb, human Ngb has an intramolecular disulfide bond that affects its oxygen affinity and protein stability. By using 2D-IR vibrational echo spectroscopy, we investigated the equilibrium protein dynamics of Ngb-CO by observing the CO spectral diffusion (time dependence of the 2D-IR line shapes) with and without the disulfide bond. Despite the similarity of the linear FTIR spectra of Ngb-CO with and without the disulfide bond, 2D-IR measurements reveal that the equilibrium sampling of different protein configurations is accelerated by disruption of the disulfide bond. The observations indicate that the intramolecular disulfide bond in Ngb acts as an inhibitor of fast protein dynamics even though eliminating it does not produce significant conformational change in the protein's structure.
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