However, the activation energy can be lowered ( and the isomerization catalyzed ) by changes that favor the single-bonded form, such as placing the peptide group in a hydrophobic environment or donating a hydrogen bond to the nitrogen atom of an X-Pro peptide group.

The hydrophobic isoprene ( e. g., farnesyl, geranyl, and geranylgeranyl groups ) and palmitoyl groups may be added to the atom of cysteine residues to anchor proteins to cellular membranes.

The heme contains a reduced iron atom, Fe2 + in the center of a highly hydrophobic, planar, porphyrin ring.

These residues, along with Il209, Trp163, and Trp164 of subunit B, and Ser27 ( C atom ) of subunit C, form the hydrophobic environment of the quinone-binding pocket ( not shown in the image ).

All of these agents share the property of being quite hydrophobic ( i. e., as liquids, they are not freely miscible in water, and as gases they dissolve in oils better than in water ).

All Mycobacterium species share a characteristic cell wall, thicker than in many other bacteria, which is hydrophobic, waxy, and rich in mycolic acids / mycolates.

All of these agents share the property of being quite hydrophobic ( i. e., as liquids, they are not freely miscible with water, and as gases they dissolve in oils better than in water ).

Carboxylic acids usually exist as dimeric pairs in nonpolar media due to their tendency to “ self-associate .” Smaller carboxylic acids ( 1 to 5 carbons ) are soluble in water, whereas higher carboxylic acids are less soluble due to the increasing hydrophobic nature of the alkyl chain.

Instead of a simple methyl group, the myristoyl group has a tail of 14 hydrophobic carbons, which make it ideal for anchoring proteins to cellular membranes.

They are made of a hydrocarbon chain that terminates with a carboxylic acid group ; this arrangement confers the molecule with a polar, hydrophilic end, and a nonpolar, hydrophobic end that is insoluble in water.

The hydrophobic tail usually consists of long fatty acid hydrocarbon chains.

While petroleum jelly is a non-polar hydrocarbon hydrophobic ( water-repelling ) and insoluble in water, glycerol ( not a hydrocarbon but an alcohol ) is the opposite: it is so strongly hydrophilic ( water-attracting ) that by continuous absorption of moisture from the air, it produces the feeling of wetness on the skin, similar to the greasiness produced by petroleum jelly.

Since the hydrocarbon portion of fatty acids is hydrophobic, these molecules can be stored in a relatively anhydrous ( water-free ) environment.

Nonylphenol features both polar and hydrophobic subunits, the phenol and the hydrocarbon tail.

Typical hydrophobic groups are saturated or unsaturated hydrocarbon chains.

The stationary phase of a reversed phase SPE cartridge is derivatized with hydrocarbon chains, which retain compounds of mid to low polarity due to the hydrophobic effect.

Of great importance to the model building effort of Watson and Crick was Rosalind Franklin's understanding of basic chemistry, which indicated that the hydrophilic phosphate-containing backbones of the nucleotide chains of DNA should be positioned so as to interact with water molecules on the outside of the molecule while the hydrophobic bases should be packed into the core.

The four polypeptide chains are bound to each other by salt bridges, hydrogen bonds, and the hydrophobic effect.

This is because some of the amino acids incorporated into proteinoid chains are more hydrophobic than others, and so proteinoids cluster together like droplets of oil in water.

The second helix binds to DNA via a number of hydrogen bonds and hydrophobic interactions, which occur between specific side chains and the exposed bases and thymine methyl groups within the major groove of the DNA.

In high-ester pectins at soluble solids content above 60 % and a pH-value between 2. 8 and 3. 6, hydrogen bonds and hydrophobic interactions bind the individual pectin chains together.

Side-chain packing methods are most useful for analyzing the protein's hydrophobic core, where side chains are more closely packed ; they have more difficulty addressing the looser constraints and higher flexibility of surface residues, which often occupy multiple rotamer conformations rather than just one.

The function of SRP was discovered by the study of processed and unprocessed immunoglobulin light chains, newly synthesized proteins in eukaryotes carry N-terminal hydrophobic signal sequences, which are bound by SRP when they emerge from the ribosome.

Loose helical amylose chains have a hydrophobic interior that can bind to hydrophobic molecules such as lipids and aromatic compounds.

The tertiary structure is the overall shape of the protein, and is usually driven by the protein's tendency to orient hydrophobic amino acid side chains internally, although hydrogen bonding, ionic interactions and disulfide bonds also help to stabilize proteins in the tertiary state Quaternary structure is the overall combination of polypeptide subunits to form the functional unit.

A promising exception to this limitation is the discovery by Marcelo Moret and Gilney Zebende that the globular compaction of protein chains by hydrophobic interactions is describable in non-Euclidean terms, with fractal critical exponents inferred from the evolution of solvent-accessible surface areas in chain segments of increasing length.

Moreover, a glutamate residue located next to body cavities filled with water molecules and lined with hydrophobic or apolar side chains has also been identified as a part of the catalytic site.

A scleroprotein occurs as an aggregate due to hydrophobic side chains that protrude from the molecule.

Although not all of the phospholipids within the raft are fully saturated, the hydrophobic chains of the lipids contained in the rafts are more saturated and tightly packed than the surrounding bilayer.

The folding is driven by the non-specific hydrophobic interactions ( the burial of hydrophobic residues from water ), but the structure is stable only when the parts of a protein domain are locked into place by specific tertiary interactions, such as salt bridges, hydrogen bonds, and the tight packing of side chains and disulfide bonds.

Structures of water-soluble proteins have a hydrophobic core in which side chains are buried from water, which stabilizes the folded state, and charged and polar side chains are situated on the solvent-exposed surface where they interact with surrounding water molecules.

Minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process, although formation of hydrogen bonds within the protein also stabilizes protein structure.

Each glycerophospholipid molecule consists of a small polar head group and two long hydrophobic chains.

The organic side chains confer hydrophobic properties while the-Si-O-Si-O-backbone is purely inorganic.

These amino acids contain an aromatic ring in their sidechain that fits into a ' hydrophobic pocket ' ( the S < sub > 1 </ sub > position ) of the enzyme.

Red: small, hydrophobic, aromatic, not Y.

Pepsin is most efficient in cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine.

Pepsin exhibits preferential cleavage for hydrophobic, preferably aromatic, residues in P1 and P1 ' positions.

It is relatively hydrophobic and aromatic in nature.

Utilized in the bacterial degradation of toxic aromatic compounds, the enzyme ’ s crystal structure indicates that intermediates are shuttled directly between active sites through a hydrophobic intermediary channel, providing an unreactive environment in which to move the reactive acetaldehyde intermediate from the aldolase active site to the acetaldehyde dehydrogenase active site.

It can bind with itself in a double helix ( A or B form ), or it can bind with another hydrophobic guest molecule such as iodine, a fatty acid, or an aromatic compound.

The energetics of DNA tertiary structure assembly were determined to be driven by the hydrophobic effect, in addition to Watson-Crick base pairing ( which is responsible for sequence selectivity ) and a significant contribution from stacking interactions between the aromatic bases.

Typical pharmacophore features include hydrophobic centroids, aromatic rings, hydrogen bond acceptors or donor, cations, and anions.