Contribution of Hydrophobic Interactions to Protein Stability
نویسندگان
چکیده
منابع مشابه
Contribution of hydrophobic interactions to protein stability.
Our goal was to gain a better understanding of the contribution of hydrophobic interactions to protein stability. We measured the change in conformational stability, Δ(ΔG), for hydrophobic mutants of four proteins: villin headpiece subdomain (VHP) with 36 residues, a surface protein from Borrelia burgdorferi (VlsE) with 341 residues, and two proteins previously studied in our laboratory, ribonu...
متن کاملContribution of hydrogen bonds to protein stability.
Our goal was to gain a better understanding of the contribution of the burial of polar groups and their hydrogen bonds to the conformational stability of proteins. We measured the change in stability, Δ(ΔG), for a series of hydrogen bonding mutants in four proteins: villin headpiece subdomain (VHP) containing 36 residues, a surface protein from Borrelia burgdorferi (VlsE) containing 341 residue...
متن کاملEngineering Hydrophobic Protein–Carbohydrate Interactions to Fine-Tune Monoclonal Antibodies
Biologically active conformations of the IgG1 Fc homodimer are maintained by multiple hydrophobic interactions between the protein surface and the N-glycan. The Fc glycan modulates biological effector functions, including antibody-dependent cellular cytotoxicity (ADCC) which is mediated in part through the activatory Fc receptor, FcγRIIIA. Consistent with previous reports, we found that site-di...
متن کاملModulation of oligonucleotide duplex and triplex stability via hydrophobic interactions.
Synthetic oligonucleotides have been proposed as a new rationally designed class of pharmaceuticals with a mechanism of action based upon a Watson-Crick and/or Hoogsteen type of base pairing with RNA or DNA regions of interest. Two series of 3'-cholesterol and/or 5'-cholesterol conjugated oligonucleotides have been synthesized. The primary structure of these compounds was conceived in a way tha...
متن کاملThe Contribution of Hydrophobic Bonds to the Thermal Stability of Proteim Conformations*
In recent discussions of protein structure and reactions, much attention has been paid to hydrophobic bonds, i.e. interactions involving nonpolar amino acid side chains of proteins (l-5). The relative number of amino acids with nonpolar side chains is large in most proteins, amounting to 35 to 50% of the total number of residues; as a consequence, the contribution of hydrophobic bonds to the st...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2011
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2011.02.053