Select All | Select None
You can now keep track of new articles from Proteins: Structure Function and Bioinformatics on your personalized homepage!
10.1002/prot.20093.abs Using a semiempirical quantum mechanical procedure (FCPAC) we have calculated the partial atomic charges of amino acids from 494 high‐resolution protein structures. To analyze the influence of the protein's environment, we considered each residue under two conditions:...
10.1002/prot.20054.abs NusG is an essential bacterial protein modulator of transcriptional elongation and termination events, and interacts directly with RNA polymerase and Rho protein. Found also in Archaea, NusG shows stretches of sequence similarity to the eukaryotic transcription elongation...
10.1002/prot.20113.abs Neuroglobin, a recently discovered globin predominantly expressed in neuronal tissue of vertebrates, binds small, gaseous ligands at the sixth coordination position of the heme iron. In the absence of an exogenous ligand, the distal histidine (His64) binds to the heme iron...
10.1002/prot.20142.abs Globular proteins are characterized by the specific and tight packing of hydrophobic side‐chains in the so‐called “hydrophobic core.” Formation of the core is key in folding, stabilization, and conformational specificity. The critical role of hydrophobic cores in...
10.1002/prot.20157.abs We study the folding thermodynamics of a β‐hairpin and two three‐stranded β‐sheet peptides using a simplified sequence‐based all‐atom model, in which folding is driven mainly by backbone hydrogen bonding and effective hydrophobic attraction. The native...
10.1002/prot.20021.abs Aldose reductase is a promising target for the treatment of diabetic complications, and as such, has become the focus of various drug design projects. As revealed by a survey of available crystal structures, the protein shows pronounced induced‐fit effects upon ligand...
10.1002/prot.20019.abs Extracting knowledge‐based statistical potential from known structures of proteins is proved to be a simple, effective method to obtain an approximate free‐energy function. However, the different compositions of amino acid residues at the core, the surface, and the...
10.1002/prot.20134.abs Introductory biochemistry texts often note that the fold of a protein is completely defined when the dihedral angles ϕ and ψ are known for each amino acid. This assertion was examined with torsion angle dynamics and simulated annealing (TAD/SA) calculations of protein G...
results per page
Save this article to read later. You can see your Read Later on your DeepDyve homepage.
To save an article, log in first, or sign up for a DeepDyve account if you don't already have one.
Sign Up Log In
To subscribe to email alerts, please log in first, or sign up for a DeepDyve account if you don't already have one.
Read and print from thousands of top scholarly journals.
Sign up with Facebook
Sign up with Google
Already have an account? Log in
To get new article updates from a journal on your personalized homepage, please log in first, or sign up for a DeepDyve account if you don't already have one.