Spin labeled ice binding compounds (IBCs) including ice binding proteins (IBPs), also called antifreeze proteins (AFPs) and their analogs are exploited to carry the paramagnetic centers for dynamic nuclear polarization (DNP), for enhancing nuclear magnetic resonance (NMR) signal intensities. Use of spin labeled IBCs to perform DNP exploits the IBCs' ability to homogeneously distribute the paramagnetic centers in frozen water solution at low temperature, leading to high DNP efficiency. Other advantages of using spin labeled IBCs include: (1) ability to cryo-protect biological samples; (2) the relative positions and orientations of the spin labeling groups in an IBC may also be cryo-preserved; (3) positions and orientations of spin labeling groups to an IBC can be selected with great freedom and without technical barrier to making multiple spin labels in an IBC; and (4) water solubilities of spin labeled IBCs are potentially high, enabling use of a solvent that is primarily water for DNP at low temperatures.

Spin labeled ice binding compounds (IBCs) including ice binding proteins (IBPs), also called antifreeze proteins (AFPs) and their analogs are exploited to carry the paramagnetic centers for dynamic nuclear polarization (DNP), for enhancing nuclear magnetic resonance (NMR) signal intensities. Use of spin labeled IBCs to perform DNP exploits the IBCs' ability to homogeneously distribute the paramagnetic centers in frozen water solution at low temperature, leading to high DNP efficiency. Other advantages of using spin labeled IBCs include: (1) ability to cryo-protect biological samples; (2) the relative positions and orientations of the spin labeling groups in an IBC may also be cryo-preserved; (3) positions and orientations of spin labeling groups to an IBC can be selected with great freedom and without technical barrier to making multiple spin labels in an IBC; and (4) water solubilities of spin labeled IBCs are potentially high, enabling use of a solvent that is primarily water for DNP at low temperatures.

The invention relates to a composition of peptides having an aminogram in which: glycine, hydroxyproline and proline are in molar quantities such that the ratio of each quantity to the sum of the molar quantities of the amino acids in the composition is comprised between 20.0% and 24.5%, between 6.0% and 12.0% and between 10.6% and 14.6%, respectively; the peptide composition comprising a quantity of peptides with a molecular weight lower than 1400 Da such that the ratio of said quantity to the quantity of peptides in the composition is less than 40%; the molecular weight and the quantity of peptides in the composition being determined by exclusion chromatography. The invention likewise relates to such a composition to be used as a drug. The invention further relates to such a composition to be used as a food supplement.

The present invention relates to methods of regulating G protein activity, and related methods for the treatment of therapeutic conditions, for example retinal degeneration, by transforming a cell with a bistable opsin to activate a G protein, and provide a phototransduction response.

An improved method of deprotection in solid phase peptide synthesis is disclosed. In particular the deprotecting composition is added in high concentration and small volume to the mixture of the coupling solution, the growing peptide chain, and any excess activated acid from the preceding coupling cycle, and without any draining step between the coupling step of the previous cycle and the addition of the deprotection composition for the successive cycle. Thereafter, the ambient pressure in the vessel is reduced with a vacuum pull to remove the deprotecting composition without any draining step and without otherwise adversely affecting the remaining materials in the vessel or causing problems in subsequent steps in the SPPS cycle.

There are disclosed hybrid proteins comprising at least one signal sequence; at least one DNA binding domain; and at least one cell penetrating peptide (CPP) domain. In embodiments the CPP domain is a TAT domain, and the DNA binding domain is a HU domain. There is also disclosed the use of the hybrid proteins to introduce exogenous DNA into target cells, and methods for introducing exogenous DNA into target cells using the hybrid proteins.

Methods to prepare recombinant adeno-associated virus (AAV) capsids with altered tropism and compositions having AAVs with altered tropism are provided.

Methods to prepare recombinant adeno-associated virus (AAV) capsids with altered tropism and compositions having AAVs with altered tropism are provided.

Improved chemodenervation agents are provided comprising polypeptide α-neurotoxins having high binding specificity and selectivity for the human muscular α1 nAChR instead of the human neuronal α7 nAChR, along with pharmaceutical compositions and methods of use.

Improved chemodenervation agents are provided comprising polypeptide α-neurotoxins having high binding specificity and selectivity for the human muscular α1 nAChR instead of the human neuronal α7 nAChR, along with pharmaceutical compositions and methods of use.