The role of context on alpha-helix stabilization: Host-guest analysis in a mixed background peptide model

被引:53
作者
Yang, JX [1 ]
Spek, EJ [1 ]
Gong, YX [1 ]
Zhou, HX [1 ]
Kallenbach, NR [1 ]
机构
[1] NYU,DEPT CHEM,NEW YORK,NY 10003
关键词
alpha-helix; CD; helix propensities; helix stability; NMR; secondary structure; synthetic peptide;
D O I
10.1002/pro.5560060614
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
The helix content of a series of peptides containing single substitutions of the 20 natural amino acids in a new designed host sequence, succinyl-YSEEEEKAKKAXAEEAEKKKK-NH2, has been determined using CD spectroscopy. This host is related to one previously studied, in which triple amino acid substitutions were introduced into a background of Glu-Lys blocks completely lacking alanine. The resulting free energies show that only Ala and Glu(-) prove to be helix stabilizing, while all other side chains are neutral or destabilizing. This agrees with results from studies of alanine-rich peptide models, but not the previous Glu-Lys block oligomers in which Leu and Met also stabilize helix. The helix propensity scale derived from the previous block oligomers correlated well with the frequencies of occurrence of different side chains in helical sequences of proteins, whereas the values from the present series do not. The role of context in determining scales of helix propensity values is discussed, and the ability of algorithms designed to predict helix structure from sequence is compared.
引用
收藏
页码:1264 / 1272
页数:9
相关论文
共 62 条
[1]   MLEV-17-BASED TWO-DIMENSIONAL HOMONUCLEAR MAGNETIZATION TRANSFER SPECTROSCOPY [J].
BAX, A ;
DAVIS, DG .
JOURNAL OF MAGNETIC RESONANCE, 1985, 65 (02) :355-360
[2]   PRACTICAL ASPECTS OF TWO-DIMENSIONAL TRANSVERSE NOE SPECTROSCOPY [J].
BAX, A ;
DAVIS, DG .
JOURNAL OF MAGNETIC RESONANCE, 1985, 63 (01) :207-213
[3]   ALPHA-HELIX PROPENSITY OF AMINO-ACIDS - RESPONSE [J].
BLABER, M ;
ZHANG, XJ ;
MATTHEWS, BW .
SCIENCE, 1993, 262 (5135) :917-918
[4]   STRUCTURAL BASIS OF AMINO-ACID ALPHA-HELIX PROPENSITY [J].
BLABER, M ;
ZHANG, XJ ;
MATTHEWS, BW .
SCIENCE, 1993, 260 (5114) :1637-1640
[5]  
CHAKRABARTTY A, 1994, PROTEIN SCI, V3, P843
[6]   LARGE DIFFERENCES IN THE HELIX PROPENSITIES OF ALANINE AND GLYCINE [J].
CHAKRABARTTY, A ;
SCHELLMAN, JA ;
BALDWIN, RL .
NATURE, 1991, 351 (6327) :586-588
[7]   2-POINT CALIBRATION OF CIRCULAR DICHROMETER WITH D-10-CAMPHORSULFONIC ACID [J].
CHEN, GC ;
YANG, JT .
ANALYTICAL LETTERS, 1977, 10 (14) :1195-1207
[8]  
Chou P Y, 1978, Adv Enzymol Relat Areas Mol Biol, V47, P45
[9]   SIDE-CHAIN ENTROPY OPPOSES ALPHA-HELIX FORMATION BUT RATIONALIZES EXPERIMENTALLY DETERMINED HELIX-FORMING PROPENSITIES [J].
CREAMER, TP ;
ROSE, GD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (13) :5937-5941
[10]   ALPHA-HELIX-FORMING PROPENSITIES IN PEPTIDES AND PROTEINS [J].
CREAMER, TP ;
ROSE, GD .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1994, 19 (02) :85-97