ArticleJournal of the American Chemical Society2011
Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Genetically encoded non-canonical amino acids reveal asynchronous dark reversion of chromophore, backbone, and side-chains in EL222.Protein science : a publication of the Protein Society · 2023Article
- Combining High-Pressure NMR and Geometrical Sampling to Obtain a Full Topological Description of Protein Folding Landscapes: Application to the Folding of Two MAX Effectors fromInternational journal of molecular sciences · 2022Article
- Extending the vibrational lifetime of azides with heavy atoms.Physical chemistry chemical physics : PCCP · 2020Article
- Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018Article
- Exploring local solvation environments of a heme protein using the spectroscopic reporter 4-cyano-l-phenylalanine.RSC advances · 2018Article
- Molecular, Local, and Network-Level Basis for the Enhanced Stiffness of Hydrogel Networks Formed from Coassembled Racemic Peptides: Predictions from Pauling and Corey.ACS central science · 2017Article
- Two-Dimensional Infrared Study of Vibrational Coupling between Azide and Nitrile Reporters in a RNA Nucleoside.The journal of physical chemistry. B · 2016Article
- When fast is better: protein folding fundamentals and mechanisms from ultrafast approaches.The Biochemical journal · 2016Review
- Meandering Down the Energy Landscape of Protein Folding: Are We There Yet?Biophysical journal · 2016Review
- Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study.Acta crystallographica. Section D, Structural biology · 2016Article
- Azidoethoxyphenylalanine as a Vibrational Reporter and Click Chemistry Partner in Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Sequence, structure, and cooperativity in folding of elementary protein structural motifs.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Theoretical Sum Frequency Generation Spectroscopy of Peptides.The journal of physical chemistry. B · 2015Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- Mapping fast protein folding with multiple-site fluorescent probes.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Fast helix formation in the B domain of protein A revealed by site-specific infrared probes.Biochemistry · 2015Article
- A molecular interpretation of 2D IR protein folding experiments with Markov state models.Biophysical journal · 2014Article
- Submillisecond mixing in a continuous-flow, microfluidic mixer utilizing mid-infrared hyperspectral imaging detection.Lab on a chip · 2014Article
- Anisotropic energy flow and allosteric ligand binding in albumin.Nature communications · 2014Article
- Effective pumping proton collection facilitated by a copper site (CuB) of bovine heart cytochrome c oxidase, revealed by a newly developed time-resolved infrared system.The Journal of biological chemistry · 2013Article
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6 authors.
Funding
Abstract
The time scale for ordering of the polypeptide backbone relative to the side chains is a critical issue in protein folding. The interplay between ordering of the backbone and ordering of the side chains is particularly important for the formation of β-sheet structures, as the polypeptide chain searches for the native stabilizing cross-strand interactions. We have studied these issues in the N-terminal domain of protein L9 (NTL9), a model protein with mixed α/β structure. We have developed a general approach for introducing site-specific IR probes for the side chains (azide) and backbone ((13)C═(18)O) using recombinant protein expression. Temperature-jump time-resolved IR spectroscopy combined with site-specific labeling enables independent measurement of the respective backbone and side-chain dynamics with single residue resolution. We have found that side-chain ordering in a key region of the β-sheet structure occurs on a slower time scale than ordering of the backbone during the folding of NTL9, likely as a result of the transient formation of non-native side-chain interactions.
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