How to measure and predict the molar absorption coefficient of a protein

By C. Pace, F. Vajdos, Lanette Fee, G. Grimsley, Theronica Gray. 1995

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Citations in the corpus

De novo protein design by deep network hallucination (2020, methodology): “Protein concentrations were determined by absorbance at 280 nm measured using a NanoDrop spectro-photometer (Thermo Scientific) using predicted extinction coefficients 33 .”
Odorant binding and conformational changes of a rat odorant-binding protein. (2004, methodology): “OBP-1F concentration was determined using UV spectroscopy employing a extinction coefficient of 14 173/M/cm at 276.3 nm, measured according to Pace et al. (1995).”
SEDPHAT – a platform for global ITC analysis and global multi-method analysis of molecular interactions (2014, background): “(For example, assigning errors arising in amino acid based extinction coefficients bounds of +/−20% may seem reasonable [67].”
From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. (2000, methodology): “One unit of enzyme activity is defined as the amount of enzyme that releases 1 µmol inorganic phosphate per minute at 37°C. Protein concentrations were determined using, for each phytase, its calculated extinction coefficient at 280 nm (for consensus phytase, 1.101) (Pace et al., 1995).”
Sampling bottlenecks in de novo protein structure prediction (2009, unknown): “The protein concentration was determined using an extinction coefficient calculated from the amino acid composition.(37) The absorbance at 280 nm was corrected for the contribution of the dye.”
The use of circular dichroism spectroscopy to study protein folding, form and function (2009, methodology): “Among the most common methods to determine the concentration of proteins is the reliable method of Edelhoch (Gill and von Hippel, 1989; Pace et al., 1995; Ramos, 2004), which was established in 1967 and has the name of its inventor.”
Preorganized secondary structure as an important determinant of fast protein folding (2001, methodology): “Backbone dynamics of (1-71)bacterioopsin studied by two-dimensional 1H- 15N NMR spectroscopy.”
Control of protein signaling using a computationally designed GTPase/GEF orthogonal pair (2012, methodology): “600 input models were selected from the 10,000 decoys from step (3), using the following criteria: The 10,000 decoys were first binned by RMSD to the flexible regions in the template (so only information of the template structure was used, as in a general application the structure of the target, the”
Nanodiamond Particles: Properties and Perspectives for Bioapplications (2009, methodology): “363 , 364 , 365 The retention of ∼ 60% hydrolytic activity of lysozyme after adsorption onto carboxylated/oxidized 100 nm NDs compared to free lysozyme in solution was earlier demonstrated by Nguyen et al.”
Computational reprogramming of homing endonuclease specificity at multiple adjacent base pairs (2010, methodology): “Protein purity and identity were verified by polyacrylamide gel electrophoresis (PAGE) and liquid chromatography mass spectrometry (LCMS), and their concentrations were determined by dividing absorbance at 280 nm by their predicted extinction coefficients (5500*Trp+1490*Tyr+125*Cys M (1)cm (1)) (23)”