SCANNING TUNNELING MICROSCOPY AND ATOMIC FORCE MICROSCOPY VISUALIZATION OF THE COMPONENTS OF THE SKELETAL-MUSCLE GLYCOGENOLYTIC COMPLEX

被引:6
作者
EDSTROM, RD
MILLER, MA
ELINGS, VB
YANG, XR
YANG, R
LEE, G
EVANS, DF
机构
[1] DIGITAL INSTRUMENTS INC,SANTA BARBARA,CA 93117
[2] UNIV MINNESOTA,CTR INTERFACIAL ENGN,MINNEAPOLIS,MN 55455
[3] UNIV MINNESOTA,DEPT BIOCHEM,MINNEAPOLIS,MN 55455
来源
JOURNAL OF VACUUM SCIENCE & TECHNOLOGY B | 1991年 / 9卷 / 02期
关键词
D O I
10.1116/1.585214
中图分类号
TM [电工技术]; TN [电子技术、通信技术];
学科分类号
0808 ; 0809 ;
摘要
The muscle glycogenolytic complex is responsible for providing access to the reserve carbohydrate energy stores in skeletal muscle during times of vigorous exercise. The complex is a set of enzymes and regulatory factors that are bound to the carbohydrate storage polymer, glycogen. These components provide the ordered synthesis and utilization of that stored form of glucose. Glycogen and the enzyme proteins, phosphorylase and phosphorylase kinase, have been imaged by atomic force microscopy (AFM) or scanning tunneling microscopy (STM). The images of all three generally correlated well with the known features of those molecules, as measured by traditional physicochemical methods. The exception for all three polymers is that the measured height by STM is in error. In each case, the molecules appear to be only about 30% of their true thickness, as measured by height above the graphite surface. It is clear that both AFM and STM will play important roles in biomedical investigation of macromolecular structures and complexes.
引用
收藏
页码:1248 / 1252
页数:5
相关论文
共 20 条
[1]   DETERMINATION OF SURFACE-TOPOGRAPHY OF BIOLOGICAL SPECIMENS AT HIGH-RESOLUTION BY SCANNING TUNNELLING MICROSCOPY [J].
BARO, AM ;
MIRANDA, R ;
ALAMAN, J ;
GARCIA, N ;
BINNIG, G ;
ROHRER, H ;
GERBER, C ;
CARRASCOSA, JL .
NATURE, 1985, 315 (6016) :253-254
[2]  
COHEN P, 1972, EUR J BIOCHEM, V34, P1
[3]   STRUCTURAL ASPECTS OF THE CATALYTIC AND REGULATORY FUNCTION OF GLYCOGEN-PHOSPHORYLASE [J].
DOMBRADI, V .
INTERNATIONAL JOURNAL OF BIOCHEMISTRY, 1981, 13 (02) :125-139
[4]   IMAGES OF SINGLE-STRANDED NUCLEIC-ACIDS BY SCANNING TUNNELLING MICROSCOPY [J].
DUNLAP, DD ;
BUSTAMANTE, C .
NATURE, 1989, 342 (6246) :204-206
[5]   VIEWING MOLECULES WITH SCANNING TUNNELING MICROSCOPY AND ATOMIC FORCE MICROSCOPY [J].
EDSTROM, RD ;
YANG, XR ;
LEE, G ;
EVANS, DF .
FASEB JOURNAL, 1990, 4 (13) :3144-3151
[6]   DIRECT OBSERVATION OF PHOSPHORYLASE-KINASE AND PHOSPHORYLASE-B BY SCANNING TUNNELING MICROSCOPY [J].
EDSTROM, RD ;
MEINKE, MH ;
YANG, XR ;
YANG, R ;
EVANS, DF .
BIOCHEMISTRY, 1989, 28 (12) :4939-4942
[7]   MUSCLE PHOSPHORYLASE-B [J].
FISCHER, EH ;
KREBS, EG .
METHODS IN ENZYMOLOGY, 1962, 5 :369-373
[8]   THE STRUCTURES AND RELATED FUNCTIONS OF PHOSPHORYLASE-A [J].
FLETTERICK, RJ ;
MADSEN, NB .
ANNUAL REVIEW OF BIOCHEMISTRY, 1980, 49 :31-61
[9]   STRUCTURE OF MALTOHEPTAOSE BY DIFFERENCE FOURIER METHODS AND A MODEL FOR GLYCOGEN [J].
GOLDSMITH, E ;
SPRANG, S ;
FLETTERICK, R .
JOURNAL OF MOLECULAR BIOLOGY, 1982, 156 (02) :411-427
[10]   REVISION OF MEYER-BERNFELD MODEL OF GLYCOGEN AND AMYLOPECTIN [J].
GUNJASMITH, Z ;
MARSHALL, JJ ;
MERCIER, C ;
SMITH, EE ;
WHELAN, WJ .
FEBS LETTERS, 1970, 12 (02) :101-+