ArticleJournal of the American Chemical Society2010
Dynamics of a myoglobin mutant enzyme: 2D IR vibrational echo experiments and simulations.
Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Do Osmolytes Impact the Structure and Dynamics of Myoglobin?Molecules (Basel, Switzerland) · 2018Article
- Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy.Chemical reviews · 2017Review
- Oscillatory Enzyme Dynamics Revealed by Two-Dimensional Infrared Spectroscopy.The journal of physical chemistry letters · 2016Article
- Histidine Orientation Modulates the Structure and Dynamics of a de Novo Metalloenzyme Active Site.Journal of the American Chemical Society · 2015Article
- Ultrafast infrared spectroscopy reveals water-mediated coherent dynamics in an enzyme active site.Chemical science · 2015Article
- Size-dependent ultrafast structural dynamics inside phospholipid vesicle bilayers measured with 2D IR vibrational echoes.Proceedings of the National Academy of Sciences of the United States of America · 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
- An optimized semiclassical approximation for vibrational response functions.The Journal of chemical physics · 2013Article
- Relationship of femtosecond-picosecond dynamics to enzyme-catalyzed H-transfer.Topics in current chemistry · 2013Review
- Three-dimensional structures by two-dimensional vibrational spectroscopy.Accounts of chemical research · 2012Article
- Protein dynamics studied with ultrafast two-dimensional infrared vibrational echo spectroscopy.Accounts of chemical research · 2012Article
- Fast dynamics of HP35 for folded and urea-unfolded conditions.The journal of physical chemistry. B · 2012Article
- Conformational dynamics and stability of HP35 studied with 2D IR vibrational echoes.Journal of the American Chemical Society · 2012Article
- Ribonuclease S dynamics measured using a nitrile label with 2D IR vibrational echo spectroscopy.The journal of physical chemistry. B · 2012Article
- 3-picolyl azide adenine dinucleotide as a probe of femtosecond to picosecond enzyme dynamics.The journal of physical chemistry. B · 2012Article
- 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
- Azido Homoalanine is a Useful Infrared Probe for Monitoring Local Electrostatistics and Sidechain Solvation in Proteins.The journal of physical chemistry letters · 2011Article
- Influence of histidine tag attachment on picosecond protein dynamics.Biochemistry · 2011Article
- Protein dynamics in cytochrome P450 molecular recognition and substrate specificity using 2D IR vibrational echo spectroscopy.Journal of the American Chemical Society · 2011Article
- Dynamics of the folded and unfolded villin headpiece (HP35) measured with ultrafast 2D IR vibrational echo spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Myoglobin (Mb) double mutant T67R/S92D displays peroxidase enzymatic activity in contrast to the wild type protein. The CO adduct of T67R/S92D shows two CO absorption bands corresponding to the A(1) and A(3) substates. The equilibrium protein dynamics for the two distinct substates of the Mb double mutant are investigated by using two-dimensional infrared (2D IR) vibrational echo spectroscopy and molecular dynamics (MD) simulations. The time-dependent changes in the 2D IR vibrational echo line shapes for both of the substates are analyzed using the center line slope (CLS) method to obtain the frequency-frequency correlation function (FFCF). The results for the double mutant are compared to those from the wild type Mb. The experimentally determined FFCF is compared to the FFCF obtained from molecular dynamics simulations, thereby testing the capacity of a force field to determine the amplitudes and time scales of protein structural fluctuations on fast time scales. The results provide insights into the nature of the energy landscape around the free energy minimum of the folded protein structure.
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