Subsite preferences of retroviral proteinases

Methods Enzymol. 1994:241:254-78. doi: 10.1016/0076-6879(94)41068-2.
No abstract available

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Aspartic Acid Endopeptidases / chemistry
  • Aspartic Acid Endopeptidases / genetics
  • Aspartic Acid Endopeptidases / metabolism*
  • Binding Sites
  • Catalysis
  • Chromatography, High Pressure Liquid
  • Gene Products, gag / metabolism
  • Gene Products, pol / metabolism
  • HIV Protease / metabolism
  • HIV-2 / enzymology
  • Hydrolysis
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Oligopeptides / chemical synthesis
  • Oligopeptides / metabolism
  • Peptide Fragments / analysis
  • Protein Conformation*
  • Protein Precursors / metabolism
  • Retroviridae / enzymology*
  • Retroviridae / genetics
  • Sequence Alignment
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity

Substances

  • Gene Products, gag
  • Gene Products, pol
  • Oligopeptides
  • Peptide Fragments
  • Protein Precursors
  • Aspartic Acid Endopeptidases
  • HIV Protease
  • protease p15