A SHORT LINEAR PEPTIDE THAT FOLDS INTO A NATIVE STABLE BETA-HAIRPIN IN AQUEOUS-SOLUTION

被引：499
作者：
BLANCO, FJ [1 ]
RIVAS, G [1 ]
SERRANO, L [1 ]
机构：
[1] CSIC,CTR INVEST BIOL,E-28006 MADRID,SPAIN
来源：
NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 09期
关键词：
D O I：
10.1038/nsb0994-584
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 conformational properties of a 16 residue peptide, corresponding to the second beta-hairpin of the B1 domain of protein G, have been studied by nuclear magnetic resonance spectroscopy (NMR). This fragment is monomeric under our experimental conditions and in pure water adopts a population containing up to 40% native-like beta-hairpin structure. The detection by NMR of a native-like beta-hairpin in aqueous solution, reported here for the first time, indicates that these structural elements may have an important role in the early steps of protein folding. It also provides a good model to study in detail the sequence determinants of beta-hairpin structure stability, as has been done with alpha-helices.
引用
收藏
页码：584 / 590
页数：7
相关论文
共 50 条
[1]   THERMODYNAMIC ANALYSIS OF THE FOLDING OF THE STREPTOCOCCAL PROTEIN-G IGG-BINDING DOMAINS B1 AND B2 - WHY SMALL PROTEINS TEND TO HAVE HIGH DENATURATION TEMPERATURES [J].
ALEXANDER, P ;
FAHNESTOCK, S ;
LEE, T ;
ORBAN, J ;
BRYAN, P .
BIOCHEMISTRY, 1992, 31 (14) :3597-3603
[2]   KINETIC-ANALYSIS OF FOLDING AND UNFOLDING THE 56-AMINO ACID IGG-BINDING DOMAIN OF STREPTOCOCCAL PROTEIN-G [J].
ALEXANDER, P ;
ORBAN, J ;
BRYAN, P .
BIOCHEMISTRY, 1992, 31 (32) :7243-7248
[3]   CONFORMATIONAL ISOMERISM OF ENDOTHELIN IN ACIDIC AQUEOUS-MEDIA - A QUANTITATIVE NOESY ANALYSIS [J].
ANDERSEN, NH ;
CHEN, CP ;
MARSCHNER, TM ;
KRYSTEK, SR ;
BASSOLINO, DA .
BIOCHEMISTRY, 1992, 31 (05) :1280-1295
[4]   SEEDING PROTEIN FOLDING [J].
BALDWIN, RL .
TRENDS IN BIOCHEMICAL SCIENCES, 1986, 11 (01) :6-9
[5]   TENDAMISTAT (12-26) FRAGMENT - NMR CHARACTERIZATION OF ISOLATED BETA-TURN FOLDING INTERMEDIATES [J].
BLANCO, FJ ;
JIMENEZ, MA ;
RICO, M ;
SANTORO, J ;
HERRANZ, J ;
NIETO, JL .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1991, 200 (02) :345-351
[6]   NMR EVIDENCE OF A SHORT LINEAR PEPTIDE THAT FOLDS INTO A BETA-HAIRPIN IN AQUEOUS-SOLUTION [J].
BLANCO, FJ ;
JIMENEZ, MA ;
HERRANZ, J ;
RICO, M ;
SANTORO, J ;
NIETO, JL .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (13) :5887-5888
[7]  
BLANCO FJ, 1994, BIOCHEMISTRY-US, V33, P6009
[8]   HELIX-COIL TRANSITION OF ISOLATED AMINO TERMINUS OF RIBONUCLEASE [J].
BROWN, JE ;
KLEE, WA .
BIOCHEMISTRY, 1971, 10 (03) :470-&
[9]   SIDE CHAIN-BACKBONE HYDROGEN-BONDING CONTRIBUTES TO HELIX STABILITY IN PEPTIDES DERIVED FROM AN ALPHA-HELICAL REGION OF CARBOXYPEPTIDASE-A [J].
BRUCH, MD ;
DHINGRA, MM ;
GIERASCH, LM .
PROTEINS-STRUCTURE FUNCTION AND GENETICS, 1991, 10 (02) :130-139
[10]   H-1-NMR PARAMETERS OF THE COMMON AMINO-ACID RESIDUES MEASURED IN AQUEOUS-SOLUTIONS OF THE LINEAR TETRAPEPTIDES H-GLY-GLY-X-L-ALA-OH [J].
BUNDI, A ;
WUTHRICH, K .
BIOPOLYMERS, 1979, 18 (02) :285-297
12345