A METHOD FOR PROBING THE TOPOGRAPHY AND INTERACTIONS OF PROTEINS - FOOTPRINTING OF MYOGLOBIN

被引：28

作者：

ZHONG, M ^{[1
]}

LIN, L ^{[1
]}

KALLENBACH, NR ^{[1
]}

机构：

[1] NYU,DEPT CHEM,NEW YORK,NY 10003

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 06期

关键词：

PROTEIN-PROTEIN INTERACTION; SURFACE MAPPING;

D O I：

10.1073/pnas.92.6.2111

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We describe a procedure for mapping residues on the surface of a protein molecule to its sequence, using a scheme that is analogous to nucleic acid footprinting. The protein is end labeled radioactively and subjected to limited proteolysis, and the products are analyzed by denaturing polyacrylamide gel electrophoresis and autoradiography. The method is tested with the heme protein myoglobin and applied to mapping the (unknown) surface of the molecule lacking the heme group: apomyoglobin. Sites of protein-protein interaction can be identified, as illustrated by footprinting the association between myoglobin and an anti-myoglobin monoclonal antibody.

引用

页码：2111 / 2115

页数：5

共 38 条

[1] MOLECULAR MECHANISMS OF ACID DENATURATION - THE ROLE OF HISTIDINE-RESIDUES IN THE PARTIAL UNFOLDING OF APOMYOGLOBIN [J].