Tyrosine fluorescence was used to monitor the denaturation of a protein. The protein used as our model system was the regulatory subunit (RSU) of aspartate transcarbamoylase from E. coli. RSU is a dimer of two identical chains with one zinc ion bound per chain. It is also a typtophan-deficient protein so tyrosine flourescence was used as a probe to monitor changes during denaturation
To evaluate their usefulness as chemical indicators of cumulative oxidative damage to proteins, we s...
<p>(A) Normalized tryptophan fluorescence intensity per tryptophan residue in untreated control or (...
Chemical denaturation was used to unfold the protein, changes in structure being monitored by the gr...
Intrinsic protein fluorescence has been used to monitor the guanidine HCI induced denaturation of E....
Two separate but overlapping projects were studied. First, the tryptophan corrected fluorescence emi...
To understand protein stability and the mechanism of protein folding, it is essential that we gain a...
The reversible denaturation of Escherichia coli alkaline phosphatase (AP) was followed by monitoring...
The TM0727 gene of Thermotoga maritima is responsible for encoding what has been reported to be a mo...
Time correlated single photon counting measurements of tryptophan (Trp) fluorescence intensity decay...
The intrinsic fluorescence of proteins arises principally from the aromatic amino acids tyrosine and...
WOS: 000323378600004PubMed ID: 24033594We developed a fluorescent protein construct by genetically f...
<p>Changes in average emission wavelength (AEW) of tryptophan fluorescence are represented as a func...
AbstractCharacterizing the denatured state ensemble is crucial to understanding protein stability an...
The fluorescent dye Nile red was used as a probe for the sensitive detection of large, denatured agg...
The UV photodissociation kinetics of tryptophan amino acid, Trp, attached to the membrane of bacteri...
To evaluate their usefulness as chemical indicators of cumulative oxidative damage to proteins, we s...
<p>(A) Normalized tryptophan fluorescence intensity per tryptophan residue in untreated control or (...
Chemical denaturation was used to unfold the protein, changes in structure being monitored by the gr...
Intrinsic protein fluorescence has been used to monitor the guanidine HCI induced denaturation of E....
Two separate but overlapping projects were studied. First, the tryptophan corrected fluorescence emi...
To understand protein stability and the mechanism of protein folding, it is essential that we gain a...
The reversible denaturation of Escherichia coli alkaline phosphatase (AP) was followed by monitoring...
The TM0727 gene of Thermotoga maritima is responsible for encoding what has been reported to be a mo...
Time correlated single photon counting measurements of tryptophan (Trp) fluorescence intensity decay...
The intrinsic fluorescence of proteins arises principally from the aromatic amino acids tyrosine and...
WOS: 000323378600004PubMed ID: 24033594We developed a fluorescent protein construct by genetically f...
<p>Changes in average emission wavelength (AEW) of tryptophan fluorescence are represented as a func...
AbstractCharacterizing the denatured state ensemble is crucial to understanding protein stability an...
The fluorescent dye Nile red was used as a probe for the sensitive detection of large, denatured agg...
The UV photodissociation kinetics of tryptophan amino acid, Trp, attached to the membrane of bacteri...
To evaluate their usefulness as chemical indicators of cumulative oxidative damage to proteins, we s...
<p>(A) Normalized tryptophan fluorescence intensity per tryptophan residue in untreated control or (...
Chemical denaturation was used to unfold the protein, changes in structure being monitored by the gr...