In NMR resonance assignment, an indispensable step in NMR protein studies, manually processed peaks from both N-labeled and C-labeled spectra are typically used as inputs. However, the use of homologous structures can allow one to use only N-labeled NMR data and avoid the added expense of using C-labeled data. We propose a novel integer programming framework for structure-based backbone resonan...

A secondary structure has been predicted for the heat shock protein HSP90 family from an aligned set of homologous protein sequences by using a transparent method in both manual and automated implementation that extracts conformational information from patterns of variation and conservation within the family. No statistically significant sequence similarity relates this family to any protein wi...

UNLABELLED A graphics package has been developed for performing statistics on interatomic distances and torsion angles in protein secondary structures (STARS) from a protein crystal structure database. It allows one to obtain both the graphical view and the text format of distributions of the distances and angles for atoms located in 10 types of protein secondary structures. STARS will facilita...

A computer program is used to analyse automatically and objectively the atomic co-ordinates of a large number of globular proteins in order to identify the regions of a-helix, p-sheet and reverse-turn secondary structure. Several different criteria for the assignment of secondary structure are tested for accuracy, reproducibility and efficiency. The most successful criterion, which is based on ...

A method for predicting the location of surface loops/turns and assigning the intervening secondary structure of the transglobular linkers in small, single domain globular proteins has been developed. Application to a set of 10 proteins of known structure indicates a high level of accuracy. The secondary structure assignment in the center of transglobular connections is correct in more than 85%...