β-sheets are prevalent repetitive secondary structures in folded proteins. β-sheets are formed by alternating peptide pleated strands linked by hydrogen bonding between the NH and CO groups of the...Springer Berlin Heidelbergdoi:10.1007/3-540-29623-9_6355Springer Berlin Heidelberg...
those prepared in buffers with a physiological salt concentration) the measurements are consistent withαS molecules in a more tightly-packed, antiparallel intramolecular conformation, and suggest a structure characterized by two twisting stacks of approximately five hydrogen-bonded intermolecularβ-sheets ...
The broad, long-term objective of the proposed project is to understand the basis of protein folding and stability. Beta sheets are a major structural component...
Cytotoxicity of these oligomers was attributed to out-of-register β-sheets present in their structure [35]. Primarily disordered Aβ oligomers were formed when the peptide was aggregated in the presence of aromatic compounds such as resveratrol or EGCG [39,41,72]. These oligomers were ...
The primary structure of a protein is the amino acid sequence of the polypeptide chain. The way the polypeptide chain forms hydrogen bonds determines the secondary structure. There are two main types of secondary structures in proteins, alpha helices and beta pleated sheets. The hydrogen bonding pa...
Medical Related to Beta sheets:Beta strand,Alpha helices beta sheet n. A secondary structure that occurs in many proteins and consists of two or more parallel adjacent polypeptide chains arranged in such a way that hydrogen bonds can form between the chains. Also calledbeta pleated sheet,pleated...
The quaternary structure of a protein is: A. A beta-pleated sheet B. Two or more distinct protein units joined together C. An alpha helix D. A beta-turn E. The amino acid sequence Which secondary structure is most likely to form first, alp...
This domain structure is often referred to as the TIM barrel, since it was first found in TIM. In the topological representation at the bottom of the figure, the α-helices are represented by rectangles and the β-sheets as arrows. The second class of α/β proteins contains an open-...
(1-40) fibrils, Aβ peptide (10-35), and Aβ peptide (1-42) fibrils are organized as β-sheets46,47. As Aβ peptide aggregation pathways are determined by the primary amino acid sequence and the intermolecular interactions, later studies in the structural organization of disease-related ...
Protein secondary structure: alpha-helices and beta-sheets, hairpins and loops, stabilization by hydrogen bonds