Three-Dimensional Solution NMR Structure of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of the Tryptophan Repressor Protein†

Biochemistry ◽  
2002 ◽  
Vol 41 (40) ◽  
pp. 11954-11962 ◽  
Author(s):  
Robert Tyler ◽  
István Pelczer ◽  
Jannette Carey ◽  
Valérie Copié
Keyword(s):  
Three Dimensional ◽  
Nmr Structure ◽  
Solution Nmr ◽  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Dimensional Solution ◽  
Repressor Protein ◽  
Temperature Sensitive Mutant ◽  
Tryptophan Repressor

scholarly journals Dynamical Studies Of A Temperature-Sensitive Mutant Of The Tryptophan Repressor Protein, L75F-TrpR

2009 ◽  
Vol 96 (3) ◽  
pp. 322a
Author(s):  
Valerie Copie ◽  
Brian Tripet ◽  
Anupam Goel ◽  
Lucas Nerbert ◽  
Jannette Carey
Keyword(s):  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Repressor Protein ◽  
Temperature Sensitive Mutant ◽  
Tryptophan Repressor

Thermal Denaturation Equilibria of TMV Coat Proteins with Chemically Defined Differences in their Primary Structure

1969 ◽  
Vol 24 (5) ◽  
pp. 613-617 ◽  
Author(s):  
H. Jockusch ◽  
R. Koberstein ◽  
R. Jaenicke
Keyword(s):  
Thermal Denaturation ◽  
Three Dimensional ◽  
Temperature Sensitive ◽  
Coat Proteins ◽  
Difference Spectra ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Melting Temperatures ◽  
Sedimentation Behavior ◽  
The Difference

Thermal denaturation of RNA free coat proteins of tobacco mosaic virus (TMV) was studied for wildtype TMV (vulgare) and the temperature-sensitive mutant, Ni 118. The ability to form soluble aggregates as well as the optical properties (ORD, UV-difference spectra), and the sedimentation behavior were used as criteria for the native state.At pH 7.5, I= 0.02 denaturation is reversible for both proteins. The ORD data indicate that the denatured proteins contain residual secondary structure. The “melting temperatures”, as defined by ORD measurements (cp = 0.02 mM), are 39.5 ± 1°C for vulgare and 27 ± 1°C for Ni 118 at pH 7.5, I= 0.02. By means of the aggregation test (cp = 0.05 mM) somewhat lower melting temperatures were found under the same solvent conditions. The difference between the primary structures of vulgare and Ni 118 proteins being a proline → leucine (pos. 20) replacement, the results suggest the cyclic structure of proline (20) to have a specific stabilizing function in the three dimensional protein structure. This conclusion is supported by preliminary experiments on a temperature-sensitive mutant with a threonine residue in pos. 20.

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