Conformations, flexibility, and interactions observed on individual membrane proteins by atomic force microscopy

Methods Cell Biol. 2002:68:257-99. doi: 10.1016/s0091-679x(02)68014-8.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / ultrastructure
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism
  • Membrane Proteins / ultrastructure
  • Microscopy, Atomic Force / instrumentation
  • Microscopy, Atomic Force / methods*
  • Models, Molecular
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Protein Structure, Tertiary*
  • Protein Subunits

Substances

  • Antibodies
  • Bacterial Proteins
  • Membrane Proteins
  • Protein Subunits