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An example of these amphiphilic molecules is the lipids that comprise the cell membrane. Another example is soap, which has a hydrophilic head and a hydrophobic tail, allowing it to dissolve in both water and oil. Hydrophilic and hydrophobic molecules are also known as polar molecules and nonpolar molecules, respectively. Some hydrophilic ...
The most favorable way for two such helices to arrange themselves in the water-filled environment of the cytoplasm is to wrap the hydrophobic strands against each other sandwiched between the hydrophilic amino acids. Thus, it is the burial of hydrophobic surfaces that provides the thermodynamic driving force for the oligomerization.
Peptide amphiphiles are a class of molecules consisting of either hydrophobic and hydrophilic peptide sequences, or a hydrophilic peptide with an attached hydrophobic group, which is usually an alkyl chain. The structure of a peptide amphiphiles has four key domains. Firstly there is a hydrophobic section, typically an alkyl chain.
An amphiphile (from the Greek αμφις amphis, both, and φιλíα philia, love, friendship), or amphipath, is a chemical compound possessing both hydrophilic (water-loving, polar) and lipophilic (fat-loving) properties. [1] Such a compound is called amphiphilic or amphipathic. Amphiphilic compounds include surfactants and detergents.
Protein design. Protein design is the rational design of new protein molecules to design novel activity, behavior, or purpose, and to advance basic understanding of protein function. [1] Proteins can be designed from scratch (de novo design) or by making calculated variants of a known protein structure and its sequence (termed protein redesign).
Active site. Organisation of enzyme structure and lysozyme example. Binding sites in blue, catalytic site in red and peptidoglycan substrate in black. (PDB: 9LYZ ) In biology and biochemistry, the active site is the region of an enzyme where substrate molecules bind and undergo a chemical reaction. The active site consists of amino acid ...
Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life. [3][4]
The heptad repeat is an example of a structural motif that consists of a repeating pattern of seven amino acids: [1] where H represents hydrophobic residues, C represents, typically, charged residues, and P represents polar (and, therefore, hydrophilic) residues. The positions of the heptad repeat are commonly denoted by the lowercase letters a ...