Global ETD Search
Search theses and dissertations gathered from participating repositories worldwide. Every result links back to the library that holds it. No account is needed.
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Showing 1 to 9 of 9 for “"β-hairpin"”.
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Computational investigations of protein dynamics and its implication in cellular functions: two cases on membrane sculpting by protein complexes and molecular origin of Parkinson's disease
… sculpting by F-BAR domains and transient β-hairpin structure in α-synuclein. Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular …
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Folding, dynamics and interaction studies of the Neuropeptide Y family.
… secondary structural elements: the α-helix and hairpin-like structure. Therefore, further analysis of the three most prevalent helical secondary structures found in nature (α-, 3₁₀-, π-helix) and the β-hairpin structure were carried out with carefully designed peptide models to characterize …
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Folding and aggregation of amyloid peptides
… pH and 293 K. Aβ(25-35) monomers mainly adopt β-hairpin conformations characterized by a β-turn formed by residues G29 and A30, and a β-sheet between residues N27–K28 and I31–I32 in equilibrium with coiled conformations. The β-hairpin conformations served as initial configurations to model …
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USING B-STRAND AND B-HAIRPIN PEPTIDOMIMETICS INDUCED BY CONSTRAINED AMINO ACIDS TO MODULATE THE AGGREGATION OF THE MICROTUBULE ASSOCIATED PROTEIN TAU: DESIGN, SYNTHESIS AND EVALUATION
… capable of stabilizing either a β-hairpin or an extended structure to modulate Tau protein aggregation. This work focuses on three distinct peptidomimetic units with the goal of highlighting the significant role of secondary structure in the selective regulation of both …
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Computational investigations of protein dynamics and its implications for biological functions
… driving force in blood clotting. Shear induces β-hairpin folding of the glycoprotein Ibα β-switch which increases affinity for binding to the von Willebrand factor, a key step in blood clot formation and wound healing. Through 2.1-μs MD simulations, we investigate the kinetics of flow-induced …
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Stability, folding and evolution of the tumour suppressor protein p16.
… 33-residue sequence motif that adopts a β-hairpin-helix-turn-helix fold. Multiple repeats stack in a linear manner to produce an elongated structure that is stabilized predominantly by short-range interactions between residues. Purely composed of four ANK repeats, p16 is the minimal …
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Investigating the protein quality control pathways that prevent protein aggregation in the social amoeba Dictyostelium discoideum
… protein with residues 61-80 structured in a β-hairpin conformation. Additionally, I found that a peptide of residues 61-70 were the minimal sequence required for SRCP1 to suppress aggregation, and a tandem repeat peptide of this sequence increased its potency. Kinetic analysis revealed that …
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Mutational analysis of the human histone chaperone, Nap1, in nucleosome disassembly at the HTLV-1 promoter
… histone interaction in vitro. Removal of the β-hairpin that is required for Nap1 oligomerization renders the protein unable to support disassembly. This suggests that the oligomeric form of Nap1 is required for nucleosome disassembly at the HTLV-1 promoter.
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Structural Analysis of Transient Receptor Potential Vanilloid Type 1 (TRPV1) Channel Protein and Proline Mimics using Computational Techniques
… is due to a hypothesized formation of stable β hairpin turn during peptide synthesis. Density functional theory (DFT) calculations were performed in order to determine the equilibrium constant (K) and total energy of peptides containing proline, pseudoproline or the proline mimic. Molecular …