Template-nucleated alanine-lysine helices are stabilized by position-dependent interactions between the lysine side chain and the helix barrel

被引:60
作者
Groebke, K [1 ]
Renold, P [1 ]
Tsang, KY [1 ]
Allen, TJ [1 ]
McClure, KF [1 ]
Kemp, DS [1 ]
机构
[1] MIT,DEPT CHEM,CAMBRIDGE,MA 02139
关键词
polypeptides; s values;
D O I
10.1073/pnas.93.9.4025
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
The helicity in water has been determined for several series of alanine-rich peptides that contain single lysine residues and that are N-terminally linked to a helix-inducing and reporting template termed Ac-Hel(1). The helix-propagating constant for alanine (s(Ala) value) that best fits the properties of these peptides lies in the range of 1.01-1.02, close to the value reported by Scheraga and coworkers [Wojcik, J., Altmann, K.-H. & Scheraga, H.A. (1990) Biopolymers 30, 121-134], but significantly lower than the value assigned by Baldwin and coworkers [Chakrabartty, A., Kortemme, T. & Baldwin, R. L. (1994) Protein Sci. 3, 843-852]. From a study of conjugates Ac-Hel(1)-Ala(n)-Lys-Ala(m)-NH2 and analogs in which the methylene portion of the lysine side chain is truncated, we find that the unusual helical stability of Ala(n)Lys peptides is controlled primarily by interactions of the lysine side chain with the helix barrel and only passively by the alanine matrix. Using H-1 NMR spectroscopy, we observe nuclear Overhauser effect crosspeaks consistent with proton-proton contacts expected for these interactions.
引用
收藏
页码:4025 / 4029
页数:5
相关论文
共 34 条
  • [1] PRACTICAL ASPECTS OF TWO-DIMENSIONAL TRANSVERSE NOE SPECTROSCOPY
    BAX, A
    DAVIS, DG
    [J]. JOURNAL OF MAGNETIC RESONANCE, 1985, 63 (01) : 207 - 213
  • [2] STRUCTURE DETERMINATION OF A TETRASACCHARIDE - TRANSIENT NUCLEAR OVERHAUSER EFFECTS IN THE ROTATING FRAME
    BOTHNERBY, AA
    STEPHENS, RL
    LEE, JM
    WARREN, CD
    JEANLOZ, RW
    [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1984, 106 (03) : 811 - 813
  • [3] AROMATIC SIDE-CHAIN CONTRIBUTION TO FAR-ULTRAVIOLET CIRCULAR-DICHROISM OF HELICAL PEPTIDES AND ITS EFFECT ON MEASUREMENT OF HELIX PROPENSITIES
    CHAKRABARTTY, A
    KORTEMME, T
    PADMANABHAN, S
    BALDWIN, RL
    [J]. BIOCHEMISTRY, 1993, 32 (21) : 5560 - 5565
  • [4] CHAKRABARTTY A, 1994, PROTEIN SCI, V3, P843
  • [5] LARGE DIFFERENCES IN THE HELIX PROPENSITIES OF ALANINE AND GLYCINE
    CHAKRABARTTY, A
    SCHELLMAN, JA
    BALDWIN, RL
    [J]. NATURE, 1991, 351 (6327) : 586 - 588
  • [6] FOLDING OF IMMUNOGENIC PEPTIDE-FRAGMENTS OF PROTEINS IN WATER SOLUTION .2. THE NASCENT HELIX
    DYSON, HJ
    RANCE, M
    HOUGHTEN, RA
    WRIGHT, PE
    LERNER, RA
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1988, 201 (01) : 201 - 217
  • [7] FURTHER-STUDIES OF THE HELIX DIPOLE MODEL - EFFECTS OF A FREE ALPHA-NH3+ OR ALPHA-COO- GROUP ON HELIX STABILITY
    FAIRMAN, R
    SHOEMAKER, KR
    YORK, EJ
    STEWART, JM
    BALDWIN, RL
    [J]. PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1989, 5 (01): : 1 - 7
  • [8] THE EFFECT OF RESONANCE OFFSET ON THE CROSS-RELAXATION RATE IN THE ROTATING FRAME
    FARMER, BT
    BROWN, LR
    [J]. JOURNAL OF MAGNETIC RESONANCE, 1987, 72 (01): : 197 - 202
  • [9] INCREASING SEQUENCE LENGTH FAVORS ALPHA-HELIX OVER 3(10)-HELIX IN ALANINE-BASED PEPTIDES - EVIDENCE FOR A LENGTH-DEPENDENT STRUCTURAL TRANSITION
    FIORI, WR
    MIICK, SM
    MILLHAUSER, GL
    [J]. BIOCHEMISTRY, 1993, 32 (45) : 11957 - 11962
  • [10] HAMILTON WC, 1994, STAT PHYSICAL SCI, P124