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

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.

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

Models of cooperativity in protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 61-70 ◽  
Keyword(s):  
Protein Folding ◽  
Molten Globule ◽  
Core Collapse ◽  
Hydrophobic Core ◽  
Model Studies ◽  
Helix Formation ◽  
Collapse Model ◽  
Folding Pathways ◽  
State Behaviour ◽  
Denatured States

What is the basis for the two-state cooperativity of protein folding? Since the 1950s, three main models have been put forward. 1. In ‘helix-coil’ theory, cooperativity is due to local interactions among near neighbours in the sequence. Helix-coil cooperativity is probably not the principal basis for the folding of globular proteins because it is not two-state, the forces are weak, it does not account for sheet proteins, and there is no evidence that helix formation precedes the formation of a hydrophobic core in the folding pathways. 2. In the ‘sidechain packing’ model, cooperativity is attributed to the jigsaw-puzzle-like complementary fits of sidechains. This too is probably not the basis of folding cooperativity because exact models and experiments on homopolymers with sidechains give no evidence that sidechain freezing is two-state, sidechain complementarities in proteins are only weak trends, and the molten globule model predicted by this model is far more native-like than experiments indicate. 3. In the ‘hydrophobic core collapse’ model, cooperativity is due to the assembly of non-polar residues into a good core. Exact model studies show that this model gives two-state behaviour for some sequences of hydrophobic and polar monomers. It is based on strong forces. There is considerable experimental evidence for the kinetics this model predicts: the development of hydrophobic clusters and cores is concurrent with secondary structure formation. It predicts compact denatured states with sizes and degrees of disorder that are in reasonable agreement with experiments.

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

O2-05-04: Hyperphosphorylation of Tau induces local polyproline II helix in the proline-rich domain

2008 ◽  
Vol 4 ◽  
pp. T141-T142
Author(s):  
Neal J. Zondlo ◽  
Agata A. Bielska ◽  
Aaron E. Lee
Keyword(s):  
Rich Domain ◽  
Polyproline Ii ◽  
Polyproline Ii Helix
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