The active site is highly basic with a hydrophobic patch. These features match with the chemical properties of the substrates. ...
Hydrophobic patches are then exposed on the protein's surface, and they interact with hydrophobic patches on other proteins. ... Hydrophobic residues predominantly occur in the globular protein core, but some exist in patches on the surface. Proteins that ... The hydrophobic patches on the protein surface generate highly ordered water shells. This results in a small decrease in ... thereby exposing hydrophobic patches on the protein surface and causing the protein to fall out of solution (aggregate and ...
... shifting it from a water-soluble form to a hydrophobic form. With the hydrophobic patches exposed, the toxin can slide into the ...
GroEL (Hsp60) is a double-ring 14mer with a hydrophobic patch at its opening; it is so large it can accommodate native folding ...
Although the acidic patches are not conserved in bacteria, the hydrophobic patch is always present. These hydrophobic and ... While the molecular surface of the protein near the copper binding site varies slightly, all plastocyanins have a hydrophobic ... acidic patches are believed to be the recognition/binding sites for the other proteins involved in electron transfer. ...
... have the same alpha 1 helix hydrophobic patch. However, it is composed of different amino acid residues as the same patch in ... The shared α 1 helix hydrophobic patch that all cyclin D's have is not responsible for recognizing the C-terminal helix. Rather ...
Naturally forming holes and cracks in hydrophobic soil patches allow for water to infiltrate the surface. These can form from ... making the soil hydrophobic. Other producers of hydrophobic coatings are contamination and industrial spillages along with soil ... Hydrophobic soil is a soil whose particles repel water. The layer of hydrophobicity is commonly found at or a few centimeters ... Hydrophobic soil is most familiarly formed when a fire or hot air disperses waxy compounds found in the uppermost litter layer ...
At least some cyclins contain a hydrophobic patch which may directly interact with substrates, conferring target specificity. ...
... possesses a relatively large hydrophobic patch close to the active site, and two residues in this hydrophobic patch, Met ... the copper atom that inhabits it is coordinated by five ligands surrounded by an extensive hydrophobic patch. The three ... "Involvement of the hydrophobic patch of azurin in the electron-transfer reactions with cytochrome C551 and nitrite reductase". ... as large hydrophobic residues in position 121 also raise the redox potential of the copper atom. Thus, the higher redox ...
Non-polar amino acid residues of NR4A2's co-regulators, SMRT and NCoR, bind to this hydrophobic patch. Analysis of tertiary ... This study also found essential structural components of this hydrophobic patch, to be the three amino acids residues, F574, ... research on the structure and found that NR4A2 does not contain a ligand-binding cavity but a patch filled with hydrophobic ...
... in which the exposed hydrophobic portions of the protein may interact with the exposed hydrophobic patches of other proteins. ... The hydrophobic patches of these aggregates can interact with other components of the cell and damage them. The hypotheses are ... This folding process is driven by the hydrophobic effect: a tendency for hydrophobic (water-fearing) portions of the protein to ... This can lead to exposed hydrophobic regions of the protein that aggregate with the same misfolded/unfolded protein or a ...
... is thus a form of "molecular switch." Both hydrophobic myristoyl groups and "basic patches" (highly positive ... Though the myristoyl group is added onto the end of the protein, in some cases it is sequestered within hydrophobic regions of ... The basic patch allows for favorable electrostatic interactions to occur between the negatively charged phospholipid heads of ... Utilizing the myristoyl-electrostatic switch, including a basic patch on the matrix protein, gag can assemble at lipid rafts at ...
This conserved region includes a negatively charged periphery and a positively charged surface, and a patch that is hydrophobic ...
"The unique proline of the Prochlorothrix hollandica plastocyanin hydrophobic patch impairs electron transfer to photosystem I ...
Some peripheral membrane proteins have a patch of hydrophobic amino acids on their surface that sticks to the membrane. In a ... Proline (Pro, P) has an alkyl side chain and could be considered hydrophobic, but because the side chain joins back onto the ... The water-soluble proteins tend to have their hydrophobic residues (Leu, Ile, Val, Phe, and Trp) buried in the middle of the ... Such modifications can also determine the localization of the protein, e.g., the addition of long hydrophobic groups can cause ...
... and binds Alk4 via a hydrophobic patch. CFC is structurally homologous to the VWFC-like domain. The CFC domain appears to play ...
... and Hydrophobic Patch in Mechanosensing Thymic Self-ligands". Journal of Biological Chemistry. 291 (49): 25292-305. doi:10.1074 ...
The toxin is an amphipathic peptide consisting of a large hydrophobic patch which is surrounded by a ring of six polar lysine ... These hydrophobic residues enable the toxin to carry an overall charge of +5. The toxin contains three intramolecular disulfide ... Therefore, GsMTx-4 is able to interact with the hydrophobic side of the lipid bilayer. It can insert itself into the membrane ... For all ICK blocker peptides, the dominating aromatic residues in the hydrophobic face are widely considered to promote the ...
In HNTX-I, the positively charged residues and a vicinal hydrophobic patch have most influence on the binding to the sodium ... HNTX-IV has a positively charged patch containing the amino acids Arg26, Lys27, His28, Arg29 and Lys32, of which Lys27, Arg29 ... A positively charged surface patch is important for hainantoxin-IV binding to voltage-gated sodium channels. J Pept Sci. 2012 ... Subtle differences in the positively charged patch can result in altered electrostatic properties, causing altered ...
The lack of stitching or stapling implies that procedures for applying glue-treated patches are potentially considerably less ... Hydrophobic light-activated adhesive (HLAA) is a type of glue that sets in seconds, but only after exposure to ultraviolet ...
Many UBDs of the UBA family bind to ubiquitin via a hydrophobic patch centred on a particular isoleucine residue (the "Ile44 ... patch"), although binding to other surface patches has been observed, for example the "Ile36 patch". Zinc finger UBDs have a ... more than one UBD cannot physically interact with the same Ile44-centered hydrophobic patch on a single ubiquitin molecule. ...
... evolving rapidly into fibrillar forms that hide exposed hydrophobic patches. p3 peptides have been analyzed in some researches ... Then, this highly hydrophobic monomer would rapidly evolve into fibrils with no soluble intermediate forms, the ones related to ... the expected energy of the Aβ-based oligomeric models of p3 is always positive and that these models expose hydrophobic patches ... So, p3 peptide oligomers would likely expose hydrophobic residues to water and would be less stable. As a consequence, p3 ...
This is achieved by a ubiquitin-interacting motif (UIM) found in a hydrophobic patch in the C-terminal region of the S5a/Rpn10 ...
... the hydrophobic core of the protein must be maintained and hydrophobic patches on the generally hydrophilic solvent-exposed ... This mutation creates a "hydrophobic patch" on the protein surface that promotes intermolecular aggregation, the molecular ... because packing is mediated by the sterics and hydrophobic interactions of the amino acid side chains near the helix interfaces ...
The RNA is anchored primarily by the binding affinity of the 5′ sensor and oriented by the hydrophobic surface patch on the S1 ...
These residues form two hydrophobic patches, a hydrophobic core, two positive patches, and a negative patch in the protein, ...
One interface interaction allows for two monomers to associate into dimers whose assembly is promoted at hydrophobic patches in ...
The conserved residues of the GYF domain create a contiguous patch of predominantly hydrophobic nature which forms an integral ...
Unfolded substrate proteins bind to a hydrophobic binding patch on the interior rim of the open cavity of GroEL, forming a ... The hydrophobic sites which were on the outside are gathered together at the top of the cis domain and bind each other. The ... The hydrophobic portion HSP60 is responsible for maintaining the unfolded conformation of the protein for transmembrane ... In its inactive state, the protein is in a hydrophobic state. When activated by ATP, the intermediate domain undergoes a ...
All of these compounds bind to the hydrophobic patch in the open conformation of cNTnC, with troponin activators promoting ... exposing a large hydrophobic patch in the open state. Likewise, the cardiac troponin regulatory domain, cNTnC, is in a closed ... cCTnC binds to helical cTnI41-60 via its large hydrophobic patch, stabilizing the Ca2+-bound open conformation of cCTnC and ... Hydrophobic binding of cNTnC to the "switch" region of troponin I, cTnI148-159, stabilizes the Ca2+-bound open conformation of ...