Expedição Alpha Helix. 1976/77

Alpha-helix Mimetics in Drug Discovery

The a-helix, first characterized by Linus Pauling in 1951 (Pauling et al., 1951), has been extensively studied due to its prevalence in structural biology (Brandon, 1991). a-Helices are the most common secondary conformation in natural proteins ( 40% of amino acids adopt helical conformations) (Ruan et al., 1990). A typical a-helix completes one rotation with 3.6 amino acid residues, each with ...

Alpha Helix Prediction Based on Evolutionary Computation

Multiple approaches have been developed in order to predict the protein secondary structure. In this paper, we propose an approach to such a problem based on evolutionary computation. The proposed approach considers various amino acids properties in order to predict the secondary structure of a protein. In particular, we will consider the hydrophobicity, the polarity and the charge of amino aci...

Alpha helix propensity of amino acids.

The role of [alpha]-, 310-, and [pi]-helix in helix[rarr]coil transitions

The conformational equilibrium between 310and -helical structure has been studied via high-resolution NMR spectroscopy by Millhauser and coworkers using the MW peptide Ac-AMAAKAWAAKA AAARA-NH2. Their 750-MHz nuclear Overhauser effect spectroscopy (NOESY) spectra were interpreted to reflect appreciable populations of 310-helix throughout the peptide, with the greatest contribution at the N and C...

Protein-protein interactions affect alpha helix stability in crowded environments.

The dense, heterogeneous cellular environment is known to affect protein stability through interactions with other biomacromolecules. The effect of excluded volume due to these biomolecules, also known as crowding agents, on a protein of interest, or test protein, has long been known to increase the stability of a test protein. Recently, it has been recognized that attractive protein-crowder in...