Sentence examples for clamping interaction from inspiring English sources

A recent NMR study was unable to detect the trans clamping interaction of complexin and therefore questioned the previous interpretation of the fluorescence resonance energy transfer and isothermal titration calorimetry data on which the trans clamping model was originally based.

Further, the intermolecular trans clamping interaction of CPX organizes the SNAREpins into a 'zig-zag' topology that is incompatible with opening a fusion pore (Krishnakumar et al., 2011; Kümmel et al., 2011).

Additionally, titration of scCPX into unblocked truncated SNARE complex revealed multiple binding sites consistent with independent binding sites for CPXcen and scCPXacc, thus describing the essential feature of the trans clamping interaction of CPX.

We also suspect that yet unknown additional interactions in the pre-fusion complex, which are not represented in our crystal structure, may further stabilize the trans clamping interaction (Cho et al., 2014; Radoff et al., 2014).

FRET analysis (using two FRET pairs with different R0 values) with 'flexible' CPX construct (CPX GPGP) has clearly demonstrated that the low FRET state corresponding to the angled conformation, which describes the trans clamping interaction, is due to discrete conformational change and not because of increased CPX flexibility.

Recently, Rizo, Rosenmund, and colleagues (Trimbuch et al., 2014) have re-examined the clamping interaction of CPX and have raised concerns regarding the interpretation of the ITC and FRET data and the use of the cell cell fusion assay as an in vitro system to study CPX clamping (Krishnakumar et al., 2011; Kümmel et al., 2011).

The locations of the entire group of 131 MCNH → SC βα-hairpin clamps are displayed in Figure 4A, with each clamp interaction represented as a bridge across two adjacent β-strands.

The observation of potent clamps formed by the neutral N228 in sIGPS and N231 in eIGPS, the β7α7 clamps, also shows that the formal negative charge on the aspartic acid H-bond acceptors in the remaining two potent βα-hairpin clamps is not determinative of the strength of the clamp interaction.

The contribution of each βα-clamp interaction to the structure of the TIM barrel proteins, sIGPS and eIGPS, was assessed by replacing the H-bond acceptor SC with alanine and monitoring the effects on the secondary and tertiary structure by far-UV and near-UV circular dichroism (CD) spectroscopy.

These results implicate the ε-β clamp interaction in the SOS phenotypes caused by the absence of ε (see Further discussion).

Our results indicate that the ε β clamp interaction is required for nalidixic acid induced SOS, such that the weak clamp binder leads to defective SOS induction following nalidixic acid.