Correlation between2H NMR Side-Chain Order Parameters and Sequence Conservation in Globular Proteins

2003 ◽  
Vol 125 (30) ◽  
pp. 9004-9005 ◽  
Author(s):  
Anthony Mittermaier ◽  
Alan R. Davidson ◽  
Lewis E. Kay
Keyword(s):  
Globular Proteins ◽  
Order Parameters ◽  
Sequence Conservation ◽  
Side Chain ◽  
Chain Order

scholarly journals On the ability of molecular dynamics force fields to recapitulate NMR derived protein side chain order parameters

2016 ◽  
Vol 25 (6) ◽  
pp. 1156-1160 ◽  
Author(s):  
Evan S. O'Brien ◽  
A. Joshua Wand ◽  
Kim A. Sharp
Keyword(s):  
Molecular Dynamics ◽  
Force Fields ◽  
Order Parameters ◽  
Side Chain ◽  
Chain Order

Structure of Escherichia coli membranes. Fatty acyl chain order parameters of inner and outer membranes and derived liposomes

Biochemistry ◽  
1980 ◽  
Vol 19 (8) ◽  
pp. 1638-1643 ◽  
Author(s):  
Hans Ulrich Gally ◽  
Gerd Pluschke ◽  
Peter Overath ◽  
Joachim Seelig
Keyword(s):  
Escherichia Coli ◽  
Acyl Chain ◽  
Fatty Acyl ◽  
Order Parameters ◽  
Fatty Acyl Chain ◽  
Outer Membranes ◽  
Chain Order

scholarly journals Analysis of the code relating sequence to conformation in globular proteins. The distribution of residue pairs in turns and kinks in the backbone chain

1974 ◽  
Vol 141 (3) ◽  
pp. 899-904 ◽  
Author(s):  
Barry Robson ◽  
Roger H. Pain
Keyword(s):  
Amino Acids ◽  
Low Frequency ◽  
Globular Proteins ◽  
Proton Donor ◽  
Side Chain ◽  
Donor Side ◽  
Different Types ◽  
Random Structures ◽  
Α Helix

1. The residue pair is considered as the fundamental unit which differentiates α-helix, β-pleated sheet and the various turns and kink structures of the protein backbone. 2. The HPLG alphabet (Robson & Pain, 1974) is used to group pairs of residues, giving 16 possible conformational pairs, all of which are found with differing frequencies in the nine proteins examined. 3. The frequencies of occurrence of the 16 different types of turn or kink are analysed in relation to the constituent amino acids. Those containing the L or G conformation are of low frequency and are grouped for purposes of this analysis. 4. The distribution of amino acids within all the conformational pairs is non-random, with distinct preferences shown by certain residues. 5. All pairs containing an L or G conformation require the presence of a glycine or a proton-donor side chain. 6. The results are discussed in terms of the determination of these ‘random’ structures by local interactions.

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