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Ion binding to biomolecules
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- Lund, Mikael (author)
- Lund University,Lunds universitet,Beräkningskemi,Enheten för fysikalisk och teoretisk kemi,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Computational Chemistry,Physical and theoretical chemistry,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- Heyda, Jan (author)
- Institute of Organic Chemistry and Biochemistry of the Academy of Sciences of the Czech Republic
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- Jungwirth, Pavel (author)
- Institute of Organic Chemistry and Biochemistry of the Academy of Sciences of the Czech Republic
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- Kunz, Werner (editor)
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- (creator_code:org_t)
- 2011-10-24
- 2009
- English 14 s.
- In: Specific Ion Effects. - : WORLD SCIENTIFIC. - 9789814271585 - 9789814468176 - 9789814271578 ; , s. 217-230
- Book chapter (peer-reviewed)
Abstract
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- We investigated specific anion binding to basic amino acid residues as well as to a range of patchy protein models. This microscopic information was subsequently used to probe protein–protein interactions for aqueous lysozyme solutions. Using computer simulations to study both atomistic and coarse grained protein molecules, it is shown that the ion–protein interaction mechanism as well as magnitude is largely controlled by the nature of the interfacial amino acid residues. Small anions interact with charged side-chains via ionpairing while larger, poorly hydrated anions are attracted to nonpolar residues due to a number of solvent-assisted mechanisms. Taking into account ion and surface specificity in a mesoscopic model for protein–protein interactions, we investigated the association of the protein lysozyme in aqueous solutions of sodium iodide and sodium chloride. As observed experimentally, it is found that ‘salting out’ of lysozyme follows the reverse Hofmeister series for pH below the iso-electric point and the direct series for pH above.
Subject headings
- NATURVETENSKAP -- Kemi -- Teoretisk kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences -- Theoretical Chemistry (hsv//eng)
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