Atomic force microscopy of biochemically tagged DNA

Journal Article · Sat May 01 00:00:00 EDT 1993 · Proceedings of the National Academy of Sciences of the United States of America; (United States)

OSTI ID:6441602

Ogletree, D F; Kolbe, W; Spengler, S; Salmeron, M ^[1]; Hansma, H G; Bezanilla, M ^[2]; Sano, T; Smith, C S; Cantor, C R ^[3]

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1. Lawrence Berkeley Laboratory, CA (United States)
2. Univ. of California, Santa Barbara (United States)
3. Boston Univ., MA (United States)

Small fragments of DNA of known length were made with the polymerase chain reaction. These fragments had biotin molecules covalently attached at their ends. They were subsequently labeled with a chimeric protein fusion between streptavidin and two immunoglobulin G-binding domains of staphyloccocal protein A. This tetrameric species was expected to bind up to four DNA molecules via their attached biotin moieties. The DNA-protein complex was deposited on mica and imaged with an atomic force microscope. The images revealed the protein chimera at the expected location at the ends of the strands of DNA as well as the expected dimers, trimers, and tetramers of DNA bound to a single protein. 25 refs., 5 figs.

• DOE Contract Number: AC03-76SF00098
• OSTI ID: 6441602
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (United States), Vol. 90:9; ISSN 0027-8424
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
DNA
MICROSCOPY
BIOCHEMISTRY
BIOTIN
DIMERS
DNA POLYMERASES
POLYMERASES
PROTEINS
AZOLES
CARBOXYLIC ACIDS
CHEMISTRY
ENZYMES
HETEROCYCLIC ACIDS
HETEROCYCLIC COMPOUNDS
IMIDAZOLES
NUCLEIC ACIDS
NUCLEOTIDYLTRANSFERASES
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANIC SULFUR COMPOUNDS
PHOSPHORUS-GROUP TRANSFERASES
TRANSFERASES
VITAMIN B GROUP
VITAMINS
550400* - Genetics