scholarly journals Microsecond and nanosecond polyproline II helix formation in aqueous nanodrops measured by mass spectrometry

2016 ◽  
Vol 52 (82) ◽  
pp. 12218-12221 ◽  
Author(s):  
Daniel N. Mortensen ◽  
Evan R. Williams
Keyword(s):  
Mass Spectrometry ◽  
Time Constants ◽  
Rapid Mixing ◽  
Helix Formation ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

The 1.5 μs and <400 ns time constants for the formation of polyproline II helix structures in 21 and 16 residue peptides, respectively, are measured using rapid mixing from theta-glass emitters coupled with mass spectrometry.

Urea Promotes Polyproline II Helix Formation:  Implications for Protein Denatured States†

Biochemistry ◽  
2005 ◽  
Vol 44 (16) ◽  
pp. 6269-6275 ◽  
Author(s):  
Shelly J. Whittington ◽  
Brian W. Chellgren ◽  
Veronique M. Hermann ◽  
Trevor P. Creamer
Keyword(s):  
Helix Formation ◽  
Polyproline Ii ◽  
Polyproline Ii Helix ◽  
Denatured States

Host−Guest Study of Left-Handed Polyproline II Helix Formation†

Biochemistry ◽  
2001 ◽  
Vol 40 (48) ◽  
pp. 14376-14383 ◽  
Author(s):  
Melissa A. Kelly ◽  
Brian W. Chellgren ◽  
Adam L. Rucker ◽  
Jerry M. Troutman ◽  
Michael G. Fried ◽  
...  
Keyword(s):  
Helix Formation ◽  
Left Handed ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

Host-guest scale of left-handed polyproline II helix formation

2003 ◽  
Vol 53 (1) ◽  
pp. 68-75 ◽  
Author(s):  
Adam L. Rucker ◽  
Cara T. Pager ◽  
Margaret N. Campbell ◽  
Joseph E. Qualls ◽  
Trevor P. Creamer
Keyword(s):  
Helix Formation ◽  
Left Handed ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

scholarly journals Allosteric Modulation of the Dopamine D2Receptor by Pro-Leu-Gly-NH2Peptidomimetics Constrained in Either a Polyproline II Helix or a Type II β-Turn Conformation

2009 ◽  
Vol 52 (7) ◽  
pp. 2043-2051 ◽  
Author(s):  
Bhooma Raghavan ◽  
Kevin J. Skoblenick ◽  
Swapna Bhagwanth ◽  
Niran Argintaru ◽  
Ram K. Mishra ◽  
...  
Keyword(s):  
Allosteric Modulation ◽  
Type Ii ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

Polyproline II Helix Is a Key Structural Motif of the Elastic PEVK Segment of Titin

Biochemistry ◽  
2001 ◽  
Vol 40 (12) ◽  
pp. 3427-3438 ◽  
Author(s):  
Kan Ma ◽  
Lou-sing Kan ◽  
Kuan Wang
Keyword(s):  
Structural Motif ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

scholarly journals Left-handed polyproline-II helix revisited: proteins causing proteopathies

2016 ◽  
Vol 35 (12) ◽  
pp. 2701-2713 ◽  
Author(s):  
Alexei A. Adzhubei ◽  
Anastasia A. Anashkina ◽  
Alexander A. Makarov
Keyword(s):  
Left Handed ◽  
Polyproline Ii ◽  
Polyproline Ii Helix

Polyproline-II Helix in Proteins: Structure and Function

2013 ◽  
Vol 425 (12) ◽  
pp. 2100-2132 ◽  
Author(s):  
Alexei A. Adzhubei ◽  
Michael J.E. Sternberg ◽  
Alexander A. Makarov
Keyword(s):  
Structure And Function ◽  
Polyproline Ii ◽  
Polyproline Ii Helix ◽  
And Function

2003 Fred Beamish Award Lecture — Exploring the dynamics of biological systems by mass spectrometry

2004 ◽  
Vol 82 (11) ◽  
pp. 1565-1580 ◽  
Author(s):  
Lars Konermann
Keyword(s):  
Mass Spectrometry ◽  
Protein Interactions ◽  
High Throughput Screening ◽  
Structural Changes ◽  
Structural Information ◽  
Ionization Mass ◽  
Time Resolved ◽  
Rapid Mixing ◽  
Esi Ms ◽  
Compound Libraries

This review describes the use of electrospray ionization mass spectrometry (ESI-MS) in conjunction with on-line rapid mixing techniques. This combination, termed "time-resolved" ESI-MS, provides a powerful approach for studying solution-phase reactions on timescales as short as a few milliseconds. Of particular interest is the application of this technique for monitoring protein folding reactions. Time-resolved ESI-MS can provide detailed information on structural changes of the polypeptide chain, while at the same time probing the occurrence of noncovalent ligand–protein interactions. Especially when used in combination with hydrogen–deuterium pulse labeling, these measurements yield valuable structural information on short-lived folding intermediates. Similar approaches can be used to monitor the dynamics of proteins under equilibrium conditions. Another important application of time-resolved ESI-MS are mechanistic studies on enzyme-catalyzed processes. These reactions can be monitored under presteady-state conditions, without requiring artificial chromophoric substrates or radioactive labeling. We also discuss the use of ESI-MS for monitoring noncovalent ligand–protein interactions by diffusion measurements. In contrast to conventional MS-based techniques, this approach does not rely on the preservation of noncovalent interactions in the gas phase. It appears that diffusion measurements by ESI-MS could become an interesting alternative to existing methods for the high throughput screening of compound libraries in the context of drug discovery.Key words: reaction intermediate, rapid mixing, kinetics, protein conformation, protein function.

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