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Research Ulrich Weininger

My research interests are structures and dynamics of proteins in general, and the dynamic of amino acid side chains in particular, with a focus on aromatic side chains.

NMR structures of proteins

The following protein structures have been solved by me or with my help using NMR spectroscopy:

methods for the study of side chain dynamics

Following methods have been developed for the study of side chain dynamics:

isotope labeling

site selective 13C labeling of proteins using erythrose site selective 13C labeling of proteins using ribose isotope labeling of aromatic side chains

NMR dynamics of methyl groups

1H and 13C CPMG relaxation dispersions of methionine 1H R1rho relaxation dispersions of methyl groups

NMR dynamics in aromatic side chains

13C relaxation experiments in aromatic side chains

13C CPMG relaxation dispersions in aromatic side chains 1H CPMG relaxation dispersions in aromatic side chains 1H CPMG relaxation dispersions in aromatic side chains 2

13C R1rho relaxation dispersions in aromatic side chains 1H R1rho relaxation dispersions in aromatic side chains

RDC mediated relaxation dispersions in aromatic side chains

side chain dynamics in proteins

research of general function of proteins based on side chain dynamics

dynamics of aromatic side chains in the active site of FKBP12

dynamic allosteric communication in the glucocorticoid receptor

energetics and dynamics of the proton shuttle of CA II

ring flips

experiments on aromatic side chain dynamics enable the identification and quantification of ring flips, which report on transient rearrangements in proteins

NMR studies of ring flips

ring flips in BPTI revisited

ring flips in the aromatic cluster of GB1

ring flips despite no chemical shift difference

transition state compressibility of ring flips

protonation kinetics of ionizable side chains

NMR relaxation enables to meassure the protonation kinetics (on & off) in ionizable side chains of proteins in a pH and pK_a dependent manner

site-specific protonation kinetics of acidic side chains

proton transfer kinetics in histidine side chains

protonation states of histidine

histidine can exist in a combination of 3 states, which can be investigated by NMR

the carbohydrate-binding site in Gal3 is preorganized proton occupancies in histidine side chains

pKa value determination

experimental pKa value determination of a hyperstable protein energetics and dynamics of the proton shuttle of CA II proton occupancies in histidine side chains

aggregation

coaggregation of Ab40 and Ab42 DNAJB6 inhibits the aggregation of Ab42 alpha synuclein aggregation sekundary nucleation

protein folding by NMR

stabilization of the native state of by pressure protein folding by NMR

PPIases

substrate recognition and catalytic mechanism of SlyD impact of distant peptide substrate residues on enzymatic activity of SlyD

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