Sequencing hydroxylethylamine-containing peptides via Edman degradation

被引:5
作者
Brewer, M
Oost, T
Sukonpan, C
Pereckas, M
Rich, DH
机构
[1] Univ Wisconsin, Dept Chem, Madison, WI 53706 USA
[2] Univ Wisconsin, Sch Pharm, Madison, WI 53706 USA
[3] Med Coll Wisconsin, Prot & Nucle Acid Shared Facil, Milwaukee, WI 53226 USA
[4] Med Coll Wisconsin, Dept Biochem, Milwaukee, WI 53226 USA
关键词
D O I
10.1021/ol026590i
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
[GRAPHICS] Hydroxyethylamine-containing peptides can be sequenced by automated Edman degradation to provide sequence information for peptide segments on either side of the peptide backbone modification.
引用
收藏
页码:3469 / 3472
页数:4
相关论文
共 25 条
[1]  
Atherton E., 1989, SOLID PHASE PEPTIDE
[2]   Molecular recognition of protein-ligand complexes: Applications to drug design [J].
Babine, RE ;
Bender, SL .
CHEMICAL REVIEWS, 1997, 97 (05) :1359-1472
[3]  
BECK JP, 2002, Patent No. 0202518
[4]   Sequencing of peptoid peptidomimetics by Edman degradation [J].
Boeijen, A ;
Liskamp, RMJ .
TETRAHEDRON LETTERS, 1998, 39 (21) :3589-3592
[5]  
COOPER JB, 1988, SPECIAL PUBLICATION, V65, P309
[6]   HUMAN RENIN - A NEW CLASS OF INHIBITORS [J].
DANN, JG ;
STAMMERS, DK ;
HARRIS, CJ ;
ARROWSMITH, RJ ;
DAVIES, DE ;
HARDY, GW ;
MORTON, JA .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1986, 134 (01) :71-77
[7]   METHOD FOR DETERMINATION OF THE AMINO ACID SEQUENCE IN PEPTIDES [J].
EDMAN, P .
ACTA CHEMICA SCANDINAVICA, 1950, 4 (02) :283-293
[8]  
Fields G.B., 2002, SYNTHETIC PEPTIDES U
[9]   SYNTHESIS OF PEPTIDE-DERIVED AMINO-ALCOHOLS .1. POTENTIAL TRANSITION-STATE INHIBITORS OF ANGIOTENSIN CONVERTING ENZYME [J].
GODFREY, JD ;
GORDON, EM ;
VONLANGEN, D ;
ENGEBRECHT, J ;
PLUSCEC, J .
JOURNAL OF ORGANIC CHEMISTRY, 1986, 51 (15) :3073-3075
[10]   DESIGN OF PEPTIDE DERIVED AMINO-ALCOHOLS AS TRANSITION-STATE ANALOG INHIBITORS OF ANGIOTENSIN CONVERTING ENZYME [J].
GORDON, EM ;
GODFREY, JD ;
PLUSCEC, J ;
VONLANGEN, D ;
NATARAJAN, S .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1985, 126 (01) :419-426