Published in Angew Chem Int Ed Engl on October 04, 2010
Site-Specific Spectroscopic Reporters of the Local Electric Field, Hydration, Structure, and Dynamics of Biomolecules. J Phys Chem Lett (2011) 1.36
Bioorthogonal chemical reporters for analyzing protein lipidation and lipid trafficking. Acc Chem Res (2011) 1.28
A solvatochromic model calibrates nitriles' vibrational frequencies to electrostatic fields. J Am Chem Soc (2012) 1.01
Two-dimensional IR spectroscopy of protein dynamics using two vibrational labels: a site-specific genetically encoded unnatural amino acid and an active site ligand. J Phys Chem B (2011) 0.98
Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. J Am Chem Soc (2011) 0.97
Site-specific infrared probes of proteins. Annu Rev Phys Chem (2015) 0.96
Sensitive, site-specific, and stable vibrational probe of local protein environments: 4-azidomethyl-L-phenylalanine. J Phys Chem B (2013) 0.89
A direct comparison of azide and nitrile vibrational probes. Phys Chem Chem Phys (2011) 0.86
Two-dimensional infrared spectroscopy of azido-nicotinamide adenine dinucleotide in water. J Chem Phys (2011) 0.85
Synthesis and Protein Incorporation of Azido-Modified Unnatural Amino Acids. RSC Adv (2014) 0.84
Azido Homoalanine is a Useful Infrared Probe for Monitoring Local Electrostatistics and Sidechain Solvation in Proteins. J Phys Chem Lett (2011) 0.83
General strategy for the bioorthogonal incorporation of strongly absorbing, solvation-sensitive infrared probes into proteins. J Phys Chem B (2014) 0.80
The Role of Electrostatic Interactions in Folding of β-Proteins. J Am Chem Soc (2016) 0.79
Pulse-chase analysis of procollagen biosynthesis by azidohomoalanine labeling. Connect Tissue Res (2014) 0.78
Two-Dimensional Infrared Study of Vibrational Coupling between Azide and Nitrile Reporters in a RNA Nucleoside. J Phys Chem B (2016) 0.77
Infrared spectroscopy: Mapping protein-protein contacts. Nat Chem (2012) 0.77
Probing the effectiveness of spectroscopic reporter unnatural amino acids: a structural study. Acta Crystallogr D Struct Biol (2016) 0.76
New method for the orthogonal labeling and purification of Toxoplasma gondii proteins while inside the host cell. MBio (2015) 0.75
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci (1995) 9.23
Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc Natl Acad Sci U S A (2001) 4.88
Electric fields at the active site of an enzyme: direct comparison of experiment with theory. Science (2006) 2.32
Vibrational Stark effects calibrate the sensitivity of vibrational probes for electric fields in proteins. Biochemistry (2003) 2.14
Stark spectroscopy: applications in chemistry, biology, and materials science. Annu Rev Phys Chem (1997) 1.94
Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures. Curr Opin Struct Biol (2001) 1.81
A genetically encoded infrared probe. J Am Chem Soc (2006) 1.71
Site-specific conversion of cysteine thiols into thiocyanate creates an IR probe for electric fields in proteins. J Am Chem Soc (2006) 1.68
Applications of 2D IR spectroscopy to peptides, proteins, and hydrogen-bond dynamics. J Phys Chem B (2009) 1.54
FTIR analysis of GPCR activation using azido probes. Nat Chem Biol (2009) 1.52
Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry (2007) 1.51
Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9. J Mol Biol (1998) 1.24
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol (2005) 1.21
Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding. Biochemistry (1998) 1.17
Beta-azidoalanine as an IR probe: application to amyloid Abeta(16-22) aggregation. J Phys Chem B (2008) 1.15
Infrared study of the stability and folding kinetics of a 15-residue beta-hairpin. J Am Chem Soc (2003) 1.12
Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J Mol Biol (2005) 1.12
Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli. Chembiochem (2008) 1.06
Azido-derivatized compounds as IR probes of local electrostatic environment: Theoretical studies. J Chem Phys (2008) 0.99
2D-IR spectroscopy: ultrafast insights into biomolecule structure and function. Chem Soc Rev (2009) 0.94
Site-specific relaxation kinetics of a tryptophan zipper hairpin peptide using temperature-jump IR spectroscopy and isotopic labeling. J Am Chem Soc (2008) 0.91
Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction. Nat Chem Biol (2011) 2.39
Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution. Proc Natl Acad Sci U S A (2009) 2.02
Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins. Protein Sci (2005) 1.91
Peptide models provide evidence for significant structure in the denatured state of a rapidly folding protein: the villin headpiece subdomain. Biochemistry (2004) 1.89
Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale. J Am Chem Soc (2003) 1.82
The flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity. Biochemistry (2010) 1.63
The unfolded state of the villin headpiece helical subdomain: computational studies of the role of locally stabilized structure. J Mol Biol (2006) 1.63
A single-point mutation converts the highly amyloidogenic human islet amyloid polypeptide into a potent fibrillization inhibitor. J Am Chem Soc (2007) 1.59
Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain. Proc Natl Acad Sci U S A (2005) 1.55
Residue specific resolution of protein folding dynamics using isotope-edited infrared temperature jump spectroscopy. Biochemistry (2007) 1.51
Probing protein dynamics using temperature jump relaxation spectroscopy. Curr Opin Struct Biol (2002) 1.49
A role for helical intermediates in amyloid formation by natively unfolded polypeptides? Phys Biol (2009) 1.49
Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain. J Mol Biol (2005) 1.47
The role of His-18 in amyloid formation by human islet amyloid polypeptide. Biochemistry (2005) 1.46
Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor. Nat Chem (2012) 1.39
A critical assessment of the role of helical intermediates in amyloid formation by natively unfolded proteins and polypeptides. Protein Eng Des Sel (2009) 1.38
Multistate folding of the villin headpiece domain. J Mol Biol (2005) 1.36
Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Anal Biochem (2005) 1.36
Advances in time-resolved approaches to characterize the dynamical nature of enzymatic catalysis. Chem Rev (2006) 1.35
Rifampicin does not prevent amyloid fibril formation by human islet amyloid polypeptide but does inhibit fibril thioflavin-T interactions: implications for mechanistic studies of beta-cell death. Biochemistry (2008) 1.32
Studies of helix fraying and solvation using 13C' isotopomers. Protein Sci (2005) 1.30
Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide. Org Lett (2005) 1.29
Temperature-dependent dynamics of the villin headpiece helical subdomain, an unusually small thermostable protein. J Mol Biol (2002) 1.28
Structural transformations in the dynamics of Michaelis complex formation in lactate dehydrogenase. Biophys J (2005) 1.27
Interpretation of p-cyanophenylalanine fluorescence in proteins in terms of solvent exposure and contribution of side-chain quenchers: a combined fluorescence, IR and molecular dynamics study. Biochemistry (2009) 1.25
Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology. Biochemistry (2007) 1.24
The helix-turn-helix motif as an ultrafast independently folding domain: the pathway of folding of Engrailed homeodomain. Proc Natl Acad Sci U S A (2007) 1.23
Mutational analysis demonstrates that specific electrostatic interactions can play a key role in the denatured state ensemble of proteins. J Mol Biol (2005) 1.21
The ability of rodent islet amyloid polypeptide to inhibit amyloid formation by human islet amyloid polypeptide has important implications for the mechanism of amyloid formation and the design of inhibitors. Biochemistry (2010) 1.21
Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides: implications for the study of amyloid formation. Protein Sci (2002) 1.20
Mechanism of IAPP amyloid fibril formation involves an intermediate with a transient β-sheet. Proc Natl Acad Sci U S A (2013) 1.20
2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure. J Am Chem Soc (2011) 1.20
Destabilization of human IAPP amyloid fibrils by proline mutations outside of the putative amyloidogenic domain: is there a critical amyloidogenic domain in human IAPP? J Mol Biol (2005) 1.19
Rapid cooperative two-state folding of a miniature alpha-beta protein and design of a thermostable variant. J Mol Biol (2003) 1.17
Strategies for extracting structural information from 2D IR spectroscopy of amyloid: application to islet amyloid polypeptide. J Phys Chem B (2009) 1.16
Toward an understanding of the role of dynamics on enzymatic catalysis in lactate dehydrogenase. Biochemistry (2002) 1.15
Role of aromatic interactions in amyloid formation by peptides derived from human Amylin. Biochemistry (2004) 1.14
Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry (2012) 1.13
Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids. Org Lett (2010) 1.13
Probing the folding and unfolding dynamics of secondary and tertiary structures in a three-helix bundle protein. Biochemistry (2004) 1.13
Fine structure analysis of a protein folding transition state; distinguishing between hydrophobic stabilization and specific packing. J Mol Biol (2005) 1.12
On the pathway of forming enzymatically productive ligand-protein complexes in lactate dehydrogenase. Biophys J (2008) 1.11
Denatured state effects and the origin of nonclassical phi values in protein folding. J Am Chem Soc (2006) 1.10
Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity. FEBS Lett (2013) 1.08
Two-dimensional infrared spectroscopy provides evidence of an intermediate in the membrane-catalyzed assembly of diabetic amyloid. J Phys Chem B (2009) 1.07
Folding intermediate in the villin headpiece domain arises from disruption of a N-terminal hydrogen-bonded network. J Am Chem Soc (2007) 1.07
Islet amyloid polypeptide toxicity and membrane interactions. Proc Natl Acad Sci U S A (2013) 1.06
Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors. J Am Chem Soc (2013) 1.06
Exploiting the right side of the Ramachandran plot: substitution of glycines by D-alanine can significantly increase protein stability. J Am Chem Soc (2004) 1.05
Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein Sci (2012) 1.05
Nanosecond temperature jump relaxation dynamics of cyclic beta-hairpin peptides. Biophys J (2003) 1.04
Characterizing septum inhibition in Mycobacterium tuberculosis for novel drug discovery. Tuberculosis (Edinb) (2008) 1.04
Combination of kinetically selected inhibitors in trans leads to highly effective inhibition of amyloid formation. J Am Chem Soc (2010) 1.04
Aggregation of islet amyloid polypeptide: from physical chemistry to cell biology. Curr Opin Struct Biol (2012) 1.04
The fluorescent amino acid p-cyanophenylalanine provides an intrinsic probe of amyloid formation. Chembiochem (2008) 1.03
Amyloid formation by pro-islet amyloid polypeptide processing intermediates: examination of the role of protein heparan sulfate interactions and implications for islet amyloid formation in type 2 diabetes. Biochemistry (2007) 1.03
Deamidation accelerates amyloid formation and alters amylin fiber structure. J Am Chem Soc (2012) 1.03
Conformational heterogeneity within the Michaelis complex of lactate dehydrogenase. J Phys Chem B (2011) 1.02
Electrostatic interactions in the denatured state ensemble: their effect upon protein folding and protein stability. Arch Biochem Biophys (2007) 1.01
NMR characterization of a peptide model provides evidence for significant structure in the unfolded state of the villin headpiece helical subdomain. Biochemistry (2006) 1.01
Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II. Biochemistry (2006) 1.00
The sulfated triphenyl methane derivative acid fuchsin is a potent inhibitor of amyloid formation by human islet amyloid polypeptide and protects against the toxic effects of amyloid formation. J Mol Biol (2010) 1.00
Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20. J Mol Biol (2011) 1.00
Rational design, structural and thermodynamic characterization of a hyperstable variant of the villin headpiece helical subdomain. Biochemistry (2007) 0.99
Direct evidence of active-site reduction and photodriven catalysis in sensitized hydrogenase assemblies. J Am Chem Soc (2012) 0.99
Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects. Biochemistry (2012) 0.99
A simple and economical method for the production of 13C,18O-labeled Fmoc-amino acids with high levels of enrichment: applications to isotope-edited IR studies of proteins. Org Lett (2007) 0.98
A two-dimensional view of the folding energy landscape of cytochrome c. Proc Natl Acad Sci U S A (2006) 0.98
Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure. J Mol Biol (2006) 0.98
Native like structure in the unfolded state of the villin headpiece helical subdomain, an ultrafast folding protein. Protein Sci (2009) 0.98
Differential ordering of the protein backbone and side chains during protein folding revealed by site-specific recombinant infrared probes. J Am Chem Soc (2011) 0.97
Energy landscape of the Michaelis complex of lactate dehydrogenase: relationship to catalytic mechanism. Biochemistry (2014) 0.97
Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation. J Biol Chem (2010) 0.96
Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure. Proc Natl Acad Sci U S A (2013) 0.96
Direct infrared detection of the covalently ring linked His-Tyr structure in the active site of the heme-copper oxidases. Biochemistry (2002) 0.95
Beyond the decoupling approximation in the model free approach for the interpretation of NMR relaxation of macromolecules in solution. J Am Chem Soc (2003) 0.95
Characterization of large peptide fragments derived from the N-terminal domain of the ribosomal protein L9: definition of the minimum folding motif and characterization of local electrostatic interactions. Biochemistry (2002) 0.95
Direct evidence of catalytic heterogeneity in lactate dehydrogenase by temperature jump infrared spectroscopy. J Phys Chem B (2014) 0.95
Contribution to stability and folding of a buried polar residue at the CARM1 methylation site of the KIX domain of CBP. Biochemistry (2003) 0.94
Rational design of potent domain antibody inhibitors of amyloid fibril assembly. Proc Natl Acad Sci U S A (2012) 0.94
The unfolded state of the C-terminal domain of the ribosomal protein L9 contains both native and non-native structure. Biochemistry (2009) 0.93
Role of aromatic interactions in amyloid formation by islet amyloid polypeptide. Biochemistry (2013) 0.93
Time-resolved vibrational spectroscopy detects protein-based intermediates in the photosynthetic oxygen-evolving cycle. Proc Natl Acad Sci U S A (2006) 0.93
Direct characterization of the folded, unfolded and urea-denatured states of the C-terminal domain of the ribosomal protein L9. J Mol Biol (2005) 0.93
pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. J Mol Biol (2002) 0.93
NMR and temperature-jump measurements of de novo designed proteins demonstrate rapid folding in the absence of explicit selection for kinetics. J Mol Biol (2003) 0.93
Modulation of p-cyanophenylalanine fluorescence by amino acid side chains and rational design of fluorescence probes of alpha-helix formation. Biochemistry (2010) 0.92