<scp>NMR</scp>
            of Membrane‐Associated Peptides and Proteins

Bader, Reto; Lerch, Mirjam; Zerbe, Oliver

doi:10.1002/9783527610754.sa03

Cited by 7 publications

(12 citation statements)

References 129 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…RLP-W and RLP-W-4Ac in solution have NOESY-unique signals of interactions between aromatic tryptophan protons (δ 7.00−7.60 ppm) with Hα tryptophan, (δ 4.60 ppm), Hδ arginine (δ 3.23 ppm), Hα glycine (δ 3.91 ppm), Hβ arginine (δ 1.86 and 1.58 ppm), and Hγ arginine (δ 1.21 ppm) (Figure S8). 87,88 These results suggest tryptophan−tryptophan and tryptophan−arginine spatial proximity consistent with the atomistic simulations reported above (Figure 2A IV). The former interactions are likely to happen through π−π interactions and the latter through cation−π and hydrogen bonding interactions, as shown in Figure 2C and in accordance with reports of similar interactions between arginine and tyrosine in other IDPs such as FUS and LAF-1.…”

Section: Expression and Purification Of Rlpssupporting

confidence: 88%

Alteration of Microstructure in Biopolymeric Hydrogels via Compositional Modification of Resilin-Like Polypeptides

Garcia

Patkar

Jovic

et al. 2021

ACS Biomater. Sci. Eng.

View full text Add to dashboard Cite

Heterogeneities in hydrogel scaffolds are known to impact the performance of cells in cell-laden materials constructs, and we have employed the phase separation of resilin-like polypeptides (RLPs) as a means to generate such materials.Here, we study the compositional features of resilin-like polypeptides (RLPs) that further enable our control of their liquid−liquid phase separation (LLPS) and how such control impacts the formation of microstructured hydrogels. The evaluation of the phase separation of RLPs in solutions of ammonium sulfate offers insights into the sequence-dependent LLPS of the RLP solutions, and atomistic simulations, along with 2D-nuclear Overhauser effect spectroscopy (NOESY) and correlated spectroscopy (COSY) 1 H NMR, suggest specific amino acid interactions that may mediate this phase behavior. The acrylamide functionalization of RLPs enables their photo-cross-linking into hydrogels and also enhances the phase separation of the polypeptides. A heating−cooling protocol promotes the formation of stable emulsions that yield different microstructured morphologies with tunable rheological properties. These findings offer approaches for choosing RLP compositions with phase behaviors that can be easily tuned with differences in temperature to control the resulting morphology and mechanical behavior of the heterogeneous hydrogels in regimes useful for biological applications.

show abstract

Section: Expression and Purification Of Rlpssupporting

confidence: 88%

Alteration of Microstructure in Biopolymeric Hydrogels via Compositional Modification of Resilin-Like Polypeptides

Garcia

Patkar

Jovic

et al. 2021

ACS Biomater. Sci. Eng.

View full text Add to dashboard Cite

show abstract

“…And here, the structural complexity of biological membranes becomes quite a challenge. Among the most prominent membrane models suitable for the peptide-membrane interaction studies, the similarity to biological membranes decreases in the order: liposomes, bicelles, mixed micelles, and micelles [6]. The NMR studies of peptides in the presence of liposomes are usually limited to the solid state due to their considerable size.…”

Section: Introductionmentioning

confidence: 99%

Thermodynamics, size, and dynamics of zwitterionic dodecylphosphocholine and anionic sodium dodecyl sulfate mixed micelles

Sikorska

Wyrzykowski

Szutkowski

et al. 2015

J Therm Anal Calorim

View full text Add to dashboard Cite

The thermodynamic properties of micellization for dodecylphosphocholine (DPC), sodium dodecyl sulfate (SDS), and their mixtures were studied using isothermal titration calorimetry. NMR relaxation measurements were used to explore molecular mobility of the DPC-containing micelles, whereas the diffusion measurements were taken to determine the micelle size. The DPC/SDS mixed systems reveal a tendency to form two kinds of micelles in buffered solution at lower temperatures. An increase in temperature as well as the transfer of the DPC/SDS mixed micelles from buffered to unbuffered solution results in only a single-step micellization process. The average size of the DPC-containing micelles is only slightly dependent on the SDS fraction. Examination of the data of spin-spin relaxation (T 2 ) shows that methylene protons on the polar headgroup of DPC and methylene protons (H1) on the hydrocarbon chain in the micellar systems studied reveal a heterogeneous dynamic behavior reflected in a twocomponent T 2 relaxation in the whole temperature range. The latter is the main constituent of the rigid interfacial layer core protecting the penetration of water into the hydrophobic interior.

show abstract

“…However, even for smaller proteins with good resonance dispersion and narrow linewidths, the process of structure determination can be very time consuming. Recent developments in membrane protein NMR studies have revived the role of structural NMR in pharmaceutical research [8]. More recently, new solid-state NMR techniques have emerged as a powerful tool to study proteins that were not accessible to solution state measurements.…”

Section: Introductionmentioning

confidence: 99%