Protein hydrogen bond

The secondary structure of a protein is determined by hydrogen bonding between CDO and N—H groups of the peptide linkages that make up the backbone of the protein. Hydrogen bonds can exist within the same protein... 

Figure 13.1 Secondary structure of proteins hydrogen bonding in 3-sheets ...

Hydrogen bonds. Hydrogen bonds (see See-tion 13.3) are responsible for ihe fnndamenlal characterislics of the a-helix and P-pleated sheet in addition, they contribnte to the final shape of a globnlar protein. Hydrogen bonds can form... 

The main molecular interactions involved in phenol-protein interactions are arbitrarily represented in Figure 9.2. A real case of flavonoid-protein hydrogen bond network is depicted in Figure 9.3. It refers to one of the rare examples of a flavonoid-protein complex... 

Protein structure is stabilized by multiple weak interactions. Hydrophobic interactions are the major contributors to stabilizing the globular form of most soluble proteins hydrogen bonds and ionic interactions are optimized in the specific structures that are thermodynamically most stable. 

In polypeptides and proteins, hydrogen bonds are of polar origin and are usually stronger than other noncovalent bonds. Both backbone amides and... 

In future high-resolution crystal structure studies of proteins, hydrogen bonding has to be analyzed in terms of two-center and three-center interactions. It should be stressed that three-center bonds may be especially important in protein dynamics because they can be regarded as transition intermediate from one two-center bond to another (see Part IV, Chap. 25). 

Ishima R, et al. Carbonyl carbon transverse relaxation dispersion measurements and ms-micros timescale motion in a protein hydrogen bond network. J. Biomol. NMR 2004 29 187-198. Ishima R, Torchia DA. Extending the range of amide proton relaxation dispersion experiments in proteins using a constant-time relaxation-compensated CPMG approach. J. Biomol. NMR 2003 25 243-248. 

The goal of this section is to describe a semiempirical model of nanoscale solvation that captures the dielectric modulation brought about by the approach of a hydrophobe to a protein hydrogen bond. In essence, the model captures the solvent-ordering effect promoted by the hydrophobe and quantifies the effect of this induced organization on the electrostatics of a pre-formed amide-carbonyl hydrogen bond. This model reproduces the crossover point in hydrogen bond dehydration... 

Figure 12.5 Stereo view of 3,5-dichloro-3 -isopropyl-thyronine bound to the thyroid hormone receptor a. Details of the binding pocket dashed lines indicate stabilizing ligand-protein hydrogen bonds. See color plates.

Schematic representation of inhibitor-protein hydrogen bonds in two classes of p38 MAP kinase inhibitors.

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