Intramolecular Dynamics of Low Molecular Weight Protein Tyrosine Phosphatase in Monomer–Dimer Equilibrium Studied by NMR: A Model for Changes in Dynamics upon Target Binding

Conformation and Dynamics of Ribosomal Stalk Protein L12 in Solution and on the Ribosome

“…The weighted mean values for the NTD and CTD (〈η xy 〉) are 6.8 ( 1.0 and 5.6 ( 0.7 s -1 , respectively. In the absence of conformational exchange, the ratio F (R 2 /η xy ) depends primarily on structural parameters that are expected to exhibit limited variability between different residues, yielding an average F value of 1.3 ( 0.1, as calculated using literature data (49). The weighted mean values for the NTD and CTD (〈F〉) are 1.59 ( 0.19 and 1.45 ( 0.10, respectively, demonstrating that exchange broadening is not significant.…”

NMR Reveals a Novel Glutaredoxin–Glutaredoxin Interaction Interface

“…[30][31][32][33][34] The N-terminal domain of the rat T-cell antigen CD2 (CD2d1), 31 the structural domain of troponin C in complex with a regulatory 40-mer polypeptide, 32 barstar 33 and low molecular mass protein tyrosine phosphatase 34 were shown to self-associate with apparent K d of the order of 1-10 mM. The NMR chemical shifts and the R 1 and R 2 relaxation rates are affected by the concentration in different ways.…”

The Solution Structure of the S.cerevisiae Ste11 MAPKKK SAM Domain and its Partnership with Ste50

“…For a detailed study of protein dynamics of a weakly oligomeric system (K d Z w1 mM) that is exclusively concentration-dependent, we refer the reader to a study of the 18 kDa low molecular mass protein tyrosine phosphatase (LMW-PTP). 42 To interfere with possible hydrophobic interactions between the Ste11-SAM and itself or its high affinity partner, Ste50-SAM, we produced seven charged variants of Ste11-SAM (I42R, V47R, Y54R, I59R, I61R, I68R, and L72R). From the structure of Ste11-SAM, each targeted hydrophobic residue was predominantly surface-exposed.…”