The Effect of Solvation on Biomolecular Conformation:  2-Amino-1-phenylethanol

2007 ◽  
Vol 111 (33) ◽  
pp. 9940-9954 ◽  
Author(s):  
Christopher M. Baker ◽  
Guy H. Grant
Keyword(s):  
Biomolecular Conformation

scholarly journals Histidine, the less interactive cousin of arginine

2019 ◽  
Vol 25 (2) ◽  
pp. 212-218 ◽  
Author(s):  
Ludovic Muller ◽  
Shelley N Jackson ◽  
Amina S Woods
Keyword(s):  
Electrostatic Interactions ◽  
Noncovalent Complex ◽  
Salt Bridge ◽  
Amino Acid Residues ◽  
Noncovalent Complexes ◽  
Post Translational Modifications ◽  
Noncovalent Bonds ◽  
Esi Mass Spectrometry ◽  
Main Factors ◽  
Biomolecular Conformation

Electrostatic interactions are one of the main factors influencing biomolecular conformation. The formation of noncovalent complexes by electrostatic interactions is governed by certain amino acid residues and post-translational modifications. It has been demonstrated that adjacent arginine forms noncovalent complex with phosphate; however, histidine noncovalent complexes have rarely been investigated. In the present work, we compare the interaction between basic epitopes (NLRRITRVN, SHHGLHSTPD) and diverse acidic and aromatic-rich peptides using both MALDI and ESI Mass spectrometry. We show that adjacent histidines can also form stable noncovalent bonds and that those bonds are probably formed by a salt bridge between the phosphate or the acid residues and the histidines. However, noncovalent complexes with the arginine epitopes form more readily and are stronger than those with histidine-containing epitopes.

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