Showing results (1-10 of 22) with videos related to
Sort By:
Pageof 3
Molekuliarnaia Biologiia|November 1, 1994
[How and why is pepsin stable and active at pH 2?]N S AndreevaBioorganicheskaia Khimiia|November 7, 2003
[How the features of three-dimensional structure of aspartate proteinases determine their properties]N S AndreevaMolekuliarnaia Biologiia|January 1, 1985
[The structure of pepsin. I. Molecular self-symmetry of the enzyme and implications for the evolution of aspartate proteinases]N S AndreevaScandinavian Journal of Clinical and Laboratory Investigation. Supplementum|January 1, 1992
Some aspects of structural studies on aspartic proteinasesN S AndreevaMolekuliarnaia Biologiia|October 24, 2002
[Conserved interactions of the active carboxyls in pepsin-like enzymes and retroviral proteases]N S Andreeva, M E PopovMolekuliarnaia Biologiia|July 4, 2006
[Interdomain interactions in aspartic proteases of higher organisms and their analogs in retroviral enzymes]N S Andreeva, G V GurskaiaMolekuliarnaia Biologiia|January 1, 1985
[The structure of pepsin. II. Structure of the enzyme active site (at 2 angstroms resolution)]A E Gushchina, N S AndreevaBiochemistry International|January 1, 1990
On the role of peripheral interactions in specificity of chymosinM G Safro, N S AndreevaProtein Science : a Publication of the Protein Society|November 21, 2001
Analysis of crystal structures of aspartic proteinases: on the role of amino acid residues adjacent to the catalytic site of pepsin-like enzymesN S Andreeva, L D RumshMolekuliarnaia Biologiia|October 24, 2002
[Molecular dynamics analysis of chymosin conformations in solution and in crystalline environment]I V Kashparov, A V Russ, N S AndreevaPageof 3