Models of higher-order structure: foldamers and beyond

被引：187

作者：

Cubberley, MS ^{[1
]}

Iverson, BL

机构：

[1] Alma Coll, Dept Chem, Alma, MI 48801 USA

[2] Univ Texas, Dept Chem & Biochem, Austin, TX 78712 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2001年 / 5卷 / 06期

基金：

美国国家科学基金会;

关键词：

D O I：

10.1016/S1367-5931(01)00261-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Folding, an attribute common to biological macromolecules such as proteins and nucleic acids, enables the formation of complex three-dimensional structure and thus enables the function of these exquisite molecular machines. Chemists are exploring the folding of natural and artificial systems with increasing enthusiasm and boldness of molecular design. The most recent achievements in the area of artificial folding molecules are described in this review.

引用

页码：650 / 653

页数：4

共 51 条

[1] Archer EA, 2001, CHEM-EUR J, V7, P2059, DOI 10.1002/1521-3765(20010518)7:10<2059::AID-CHEM2059>3.3.CO
[2] 2-9
[3] ARMITAGE BA, 2000, ANNU REP PROG CHEM B, V96, P187
[4] AVIDSSON PI, 2001, CHEM COMMUN, P649
[5] De novo design of a monomeric helical β-peptide stabilized by electrostatic interactions
Cheng, RP
DeGrado, WF
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (21) : 5162 - 5163
[6] CHITTARANJAN D, 2001, BIOPOLYMERS, V58, P335
[7] CORBIN PS, 2001, IN PRESS J AM CHEM S
[8] First rigid peptide foldamers with an alternating cis-trans amide sequence. An oligomeric building block for the construction of new helices, large-ring cyclic correlates, and nanotubes
Crisma, M
Moretto, A
Toniolo, C
Kaczmarek, K
Zabrocki, J
[J]. MACROMOLECULES, 2001, 34 (14) : 5048 - 5052
[9] Interplay between hydrophobic cluster and loop propensity in β-hairpin formation
Espinosa, JF
Muñoz, V
Gellman, SH
[J]. JOURNAL OF MOLECULAR BIOLOGY, 2001, 306 (03) : 397 - 402
[10] A parallel β-sheet model system that folds in water
Fisk, JD
Gellman, SH
[J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2001, 123 (02) : 343 - 344

← 1 2 3 4 5 6 →