Accession Number:

ADA230225

Title:

Determination of the Structural Basis of Antibody Diversity Using NMR

Descriptive Note:

Annual rept. Dec 1989-Dec 1990

Corporate Author:

STANFORD UNIV CA

Personal Author(s):

• McConnell, Harden M.

Report Date:

1990-12-14

Pagination or Media Count:

46.0

Abstract:

A number of interesting discoveries have been made in our recent study of the monoclonal anti-spin label antibody AN02. a Structure-Kinetics A tyrosine residue, Tyr31L, takes on one of two possible conformations when dinitrophenyl hapten binds. When the hapten dissociates, this tyrosine rotates rapidly. b AN02 is an auto antibody whose dimerization involves Tyr 31L and is blocked by hapten. c The technique of spin-label titration to measure spin- to-proton distances has been verified experimentally. This has required two definitive proton resonance signal assignments for tyrosine resonances in the combining site, and comparison with the crystallographic results Leahy Fox, to be published. d Chemical shift calculations using ring current shielding calculations have proven remarkably accurate and useful. In addition to the above, a number of single site mutations have been prepared, expressed, and NMR spectra taken. JS

Descriptors:

• *ANTIBODIES
• SITES
• PROTONS
• MUTATIONS
• SIGNALS
• RESONANCE
• CHEMICAL SHIFTS
• RINGS
• AUTOMATIC
• CRYSTALLOGRAPHY
• DIMERS
• TYROSINE
• COMPUTATIONS
• SHIELDING

Subject Categories:

• Polymer Chemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE