NMR AND PROTEIN-FOLDING - EQUILIBRIUM AND STOPPED-FLOW STUDIES

被引:69
作者
FRIEDEN, C
HOELTZLI, SD
ROPSON, IJ
机构
[1] Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St Louis, Missouri
[2] Department of Biological Chemistry, Penn State University College of Medicine, Hershey, Pennsylvania
关键词
F-19 NMR SPECTRA; HYDROGEN DEUTERIUM EXCHANGE; PROTEIN FOLDING; PROTEIN INTERMEDIATES; STOPPED-FLOW STUDIES;
D O I
10.1002/pro.5560021202
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
NMR studies are now unraveling the structure of intermediates of protein folding using hydrogen-deuterium exchange methodologies. These studies provide information about the time dependence of formation of secondary structure. They require the ability to assign specific resonances in the NMR spectra to specific amide protons of a protein followed by experiments involving competition between folding and exchange reactions. Another approach is to use F-19-substituted amino acids to follow changes in side-chain environment upon folding. Current techniques of molecular biology allow assignments of F-19 resonances to specific amino acids by site-directed mutagenesis. It is possible to follow changes and to analyze results from F-19 spectra in real time using a stopped-flow device incorporated into the NMR spectrometer.
引用
收藏
页码:2007 / 2014
页数:8
相关论文
共 66 条
[1]   STRUCTURAL STUDIES OF A FOLDING INTERMEDIATE OF BOVINE PANCREATIC RIBONUCLEASE-A BY CONTINUOUS RECYCLED FLOW [J].
ADLER, M ;
SCHERAGA, HA .
BIOCHEMISTRY, 1988, 27 (07) :2471-2480
[2]  
AKASAKA K, 1991, Journal of Biomolecular NMR, V1, P65, DOI 10.1007/BF01874569
[3]  
ALBER T, 1989, ANNU REV BIOCHEM, V58, P765, DOI 10.1146/annurev.biochem.58.1.765
[4]   KINETICS OF FORMATION OF NATIVE RIBONUCLEASE DURING OXIDATION OF REDUCED POLYPEPTIDE CHAIN [J].
ANFINSEN, CB ;
HABER, E ;
SELA, M ;
WHITE, FH .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1961, 47 (09) :1309-+
[5]  
BALDWIN RL, 1991, CIBA F SYMP, V161, P190
[6]   PULSED H/D-EXCHANGE STUDIES OF FOLDING INTERMEDIATES [J].
BALDWIN, RL .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1993, 3 (01) :84-91
[7]   CHARACTERIZATION OF A PARTLY FOLDED PROTEIN BY NMR METHODS - STUDIES ON THE MOLTEN GLOBULE STATE OF GUINEA-PIG ALPHA-LACTALBUMIN [J].
BAUM, J ;
DOBSON, CM ;
EVANS, PA ;
HANLEY, C .
BIOCHEMISTRY, 1989, 28 (01) :7-13
[8]   BAYESIAN-ANALYSIS .1. PARAMETER-ESTIMATION USING QUADRATURE NMR MODELS [J].
BRETTHORST, GL .
JOURNAL OF MAGNETIC RESONANCE, 1990, 88 (03) :533-551
[9]   EARLY HYDROGEN-BONDING EVENTS IN THE FOLDING REACTION OF UBIQUITIN [J].
BRIGGS, MS ;
RODER, H .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (06) :2017-2021
[10]   KINETIC RESOLUTION OF PEPTIDE-BOND AND SIDE-CHAIN FAR-UV CIRCULAR-DICHROISM DURING THE FOLDING OF HEN EGG-WHITE LYSOZYME [J].
CHAFFOTTE, AF ;
GUILLOU, Y ;
GOLDBERG, ME .
BIOCHEMISTRY, 1992, 31 (40) :9694-9702