The chemistry of amino acid side chains is critical to protein structure because ... side chains can form ionic bonds, and polar amino acids are capable of forming hydrogen bonds.

EPFL researchers have developed a computational method to explicitly consider the impact of water while designing membrane receptors with enhanced stability and signaling, paving the way for novel ...

Executing the generated PyMOL commands to visualize hydrogen-bonds in PyMOL After obtaining the commands for creating the H-bond visualization in PyMOL (see Step 2), open the protein and ligand ...

The Protein Recognition Index (PRI) measures the similarity between H-bonding features in a given complex (predicted or designed) and the characteristic H-bond trends from crystallographic complexes ...

These include wobble base pairs, such as G-U and I-A (inosine-adenine), which have a slightly different geometry and hydrogen bonding pattern. Non-Watson-Crick base pairs can play important roles in ...

The structure of the β-sheets is strengthened by hydrogen bonds, which remain stable throughout the functional life of the ...

Protein folding is the process ... stabilized by hydrogen bonding and disulphide bridges, and then tertiary structure. During the pathogenesis of Parkinson’s disease (PD), α-synuclein pathology ...

Uracil forms hydrogen bonds with adenine in RNA, contributing to the molecule's structure and function ... the building blocks of proteins. For example, the codon UUU codes for the amino acid ...

Free RNA nucleotides form hydrogen bonds with ... the correct shape and becomes a protein. Peptide bonds form between the adjacent amino acids to finalise the structure.

These dipoles enable hydrogen bonding between the polypeptide backbone of different parts of the same protein chain, which drives the formation of the protein's secondary structure. This bonding pulls ...