Aspects of native proteins are retained in vacuum

被引：201

作者：

Ruotolo, Brandon T. ^{[1
]}

Robinson, Carol V. ^{[1
]}

机构：

[1] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2006年 / 10卷 / 05期

关键词：

D O I：

10.1016/j.cbpa.2006.08.020

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：

It is now well established that protein complexes can be maintained in the gas phase, under the reduced pressure conditions experienced Within mass spectrometers. This remains an intriguing phenomenon, given the importance placed on water molecules in stabilizing protein structure. As a consequence, the overall structure of protein molecules and their complexes in the gas phase continues to stimulate much research. The eventual outcomes of this research will not only increase the number of applications of mass spectrometry to structural biology, but will also enhance our understanding of the interactions important for maintaining protein complexes in the absence of bulk solvent.

引用

页码：402 / 408

页数：7

共 37 条

[1] Polydispersity of a mammalian chaperone:: Mass spectrometry reveals the population of oligomers in αB-crystallin [J].

Aquilina, JA ;

Benesch, JLP ;

Bateman, OA ;

Slingsby, C ;

Robinson, CV .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (19) :10611-10616

[2] Evidence for unfolding and refolding of gas-phase cytochrome c ions in a Paul trap [J].

Badman, ER ;

Myung, S ;

Clemmer, DE .

JOURNAL OF THE AMERICAN SOCIETY FOR MASS SPECTROMETRY, 2005, 16 (09) :1493-1497

[3] Monitoring structural changes of proteins in an ion trap over ∼10-200 ms:: Unfolding transitions in cytochrome c ions [J].

Badman, ER ;

Hoaglund-Hyzer, CS ;

Clemmer, DE .

ANALYTICAL CHEMISTRY, 2001, 73 (24) :6000-6007

[4] Amyloid β-protein monomer structure:: A computational and experimental study [J].

Baumketner, A ;

Bernstein, SL ;

Wyttenbach, T ;

Bitan, G ;

Teplow, DB ;

Bowers, MT ;

Shea, JE .

PROTEIN SCIENCE, 2006, 15 (03) :420-428

[5] Mass spectrometry of macromolecular assemblies: preservation and dissociation [J].

Benesch, JL ;

Robinson, CV .

CURRENT OPINION IN STRUCTURAL BIOLOGY, 2006, 16 (02) :245-251

[6] Tandem mass spectrometry reveals the quaternary organization of macromolecular assemblies [J].

Benesch, Justin L. P. ;

Aquilina, J. Andrew ;

Ruotolo, Brandon T. ;

Sobott, Frank ;

Robinson, Carol V. .

CHEMISTRY & BIOLOGY, 2006, 13 (06) :597-605

[7] Amyloid β-protein:: Monomer structure and early aggregation states of Aβ42 and its Pro19 alloform [J].

Bernstein, SL ;

Wyttenbach, T ;

Baumketner, A ;

Shea, JE ;

Bitan, G ;

Teplow, DB ;

Bowers, MT .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2005, 127 (07) :2075-2084

[8] The thermal unfolding of native cytochrome c in the transition from solution to gas phase probed by native electron capture dissociation [J].

Breuker, K ;

McLafferty, FW .

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2005, 44 (31) :4911-4914

[9] Nonergodic and conformational control of the electron capture dissociation of protein cations [J].

Breuker, K ;

Oh, HB ;

Lin, C ;

Carpenter, BK ;

McLafferty, FW .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2004, 101 (39) :14011-14016

[10] Deuterium exchange reactions as a probe of biomolecule structure. Fundamental studies of cas phase H/D exchange reactions of protonated glycine oligomers with D2O, CD3OD, CD3CO2D, and ND3 [J].

Campbell, S ;

Rodgers, MT ;

Marzluff, EM ;

Beauchamp, JL .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1995, 117 (51) :12840-12854

← 1 2 3 4 →