Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins

Mach, H.; Middaugh, C. Russell; Lewis, Randy

doi:10.1016/0003-2697(92)90279-g

Cited by 472 publications

(316 citation statements)

References 15 publications

Supporting

Mentioning

307

Contrasting

Unclassified

Order By: Relevance

“…This shows that the combination o f t values that gives the best fit using the least-squares program of Johnson and Frasier (1985) does not give the minimum value for the avevodev. Note also that the E values that Mach et al (1992) derived from a similar analysis of a list of 81 measured E values for 32 different proteins gave ave%dev = 3.860%. This shows that quite different sets o f t values for Trp, Tyr, and cystine can give comparable values for aveyodev.…”

Section: Predicting the Absorption Coefficient Of A Proteinmentioning

confidence: 87%

“…Similar but less extensive tables were compiled by Wetlaufer (1962), Gill and von Hippel (1989), and Mach et al (1992). These tables all contained errors, and there are surely some errors in our table, but we doubt that they will significantly change the average t values we derive from our analysis.…”

Section: Cn Pace Et Almentioning

confidence: 89%

“…Some of the entries were taken from tables in other papers: 1-1 1 are from Table V in Wetlaufer (1962); 18-36 are from Table 3 in Gill and von Hippel (1989); and 37-47 are from Table 1 in Mach et al (1992). In the latter two tables, we averaged the most reliable values when more than one t value was given.…”

Section: Cn Pace Et Almentioning

confidence: 99%

“…In the last column in Table 5 The only Trp-containing protein that gave a percent deviation greater than 10% was a-B,-crystallin (entry 42 in Table 5 ) . This t value came from the list of Mach et al (1992), and they point out that the light-scattering correction for this protein was 7%, greater than for any other protein in their list. Thus, the E value for this protein is surely less reliable than most.…”

Section: Predicting the Absorption Coefficient Of A Proteinmentioning

confidence: 99%

See 3 more Smart Citations

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

et al. 1995

View full text Add to dashboard Cite

The molar absorption coefficient, E, of a protein is usually based on concentrations measured by dry weight, nitrogen, or amino acid analysis. The studies reported here suggest that the Edelhoch method is the best method for measuring E for a protein. (This method is described by Gill and von Hippel [1989, Anal Biochem 182:319-3261 and is based on data from Edelhoch [ , Biochemistry 6:1948.) The absorbance of a protein at 280 nm depends on the content of Trp, Tyr, and cystine (disulfide bonds). The average E values for these chromophores in a sample of 18 well-characterized proteins have been estimated, and the E values in water, propanol, These ~(280) values are quite reliable for proteins containing Trp residues, and less reliable for proteins that do not. However, the Edelhoch method is convenient and accurate, and the best approach is to measure rather than predict E .

show abstract

Section: Predicting the Absorption Coefficient Of A Proteinmentioning

confidence: 87%

Section: Cn Pace Et Almentioning

confidence: 89%

Section: Cn Pace Et Almentioning

confidence: 99%

Section: Predicting the Absorption Coefficient Of A Proteinmentioning

confidence: 99%

See 2 more Smart Citations

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

et al. 1995

View full text Add to dashboard Cite

show abstract

“…All other materials were from Merck (Darmstadt, Germany). a-Lactalbumin stock concentrations were determined spectroscopically at 280 nm using an E 1% of 20.3 calculated according to Mach et al (1992)). …”

Section: Materials and General Analytical Methodsmentioning

confidence: 99%

The effect of protein stability on protein–monoglyceride interactions

Boots

Chupin

Killian

et al. 2002

Chemistry and Physics of Lipids

View full text Add to dashboard Cite

We have previously shown that proteins such as b-lactoglobulin and lysozyme insert into monoglyceride monolayers and are able to induce an L b to coagel phase transition in monoglyceride bilayers. These studies gave a first indication that protein stability could be an important factor for these interactions. This study therefore aims at further investigating the potential role of protein stability on protein Á/monoglyceride interactions. To this end we studied the interaction of stable and destabilized a-lactalbumin with monostearoylglycerol. Our results show that protein stability is important for the insertion of proteins into a monostearoylglycerol monolayer, such that the lower the stability of the protein the better the protein inserts. In marked contrast to b-lactoglobulin and lysozyme we found that destabilized alactalbumin does not induce the L b to coagel phase transition in monoglyceride bilayers. We propose that this is due to an increased surface coverage by the protein which could result from the unfolding of the protein upon binding to the interface. #

show abstract