@ARTICLE{Horovitz1992560,
author={Horovitz, A. and Matthews, J.M. and Fersht, A.R.},
title={α-Helix stability in proteins. II. Factors that influence stability at an internal position},
journal={Journal of Molecular Biology},
year={1992},
volume={227},
number={2},
pages={560-568},
doi={10.1016/0022-2836(92)90907-2},
note={cited By 229},
url={https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026674251&doi=10.1016%2f0022-2836%2892%2990907-2&partnerID=40&md5=085699b34d6dcbe5576199a6445212e0},
affiliation={MRC Unit for Protein Function, Design Cambridge Centre for Protein Engineering, Department of Chemistry University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom},
abstract={The solvent-exposed residue Ala32 in the second α-helix of barnase was replaced by all other naturally occurring amino acids and the concomitant effects on the protein stability were determined. The results are assumed to reflect both the distinct conformational preferences of the different amino acids and also possible intrahelical interactions. The conformational preferences may be fully rationalized by invoking only a few physical principles. The results agree well with recently experimentally determined ran-korder of helix-forming tendencies determined on a model peptide. There is very weak correlation between the results and the experimental host-guest values. There is a weak correlation between our results and the statistical helix propensities and a slightly better correlation with the positional-dependent statistical parameters of J. S. Richardson, and D. C. Richardson. © 1992.},
author_keywords={barnase;  protein folding;  protein stability;  α-helix},
keywords={alanine;  amino acid;  ribonuclease, amino acid substitution;  article;  chemical structure;  priority journal;  protein conformation;  protein folding;  protein secondary structure;  protein stability;  statistical analysis, Amino Acid Sequence;  Amino Acids;  Base Sequence;  DNA;  Electrochemistry;  Enzyme Stability;  Hydrogen Bonding;  Molecular Sequence Data;  Mutagenesis;  Protein Conformation;  Protein Denaturation;  Ribonucleases;  Solvents;  Thermodynamics},
correspondence_address1={Horovitz, A.; MRC Unit for Protein Function, Design Cambridge Centre for Protein Engineering, Department of Chemistry University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom},
issn={00222836},
coden={JMOBA},
pubmed_id={1404369},
language={English},
abbrev_source_title={J. Mol. Biol.},
document_type={Article},
source={Scopus},
}

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Factors that influence stability at an internal position","journal":"Journal of Molecular Biology","year":"1992","volume":"227","number":"2","pages":"560-568","doi":"10.1016/0022-2836(92)90907-2","note":"cited By 229","url":"https://www.scopus.com/inward/record.uri?eid=2-s2.0-0026674251&doi=10.1016%2f0022-2836%2892%2990907-2&partnerID=40&md5=085699b34d6dcbe5576199a6445212e0","affiliation":"MRC Unit for Protein Function, Design Cambridge Centre for Protein Engineering, Department of Chemistry University of Cambridge, Lensfield Road, Cambridge, CB2 1EW, United Kingdom","abstract":"The solvent-exposed residue Ala32 in the second α-helix of barnase was replaced by all other naturally occurring amino acids and the concomitant effects on the protein stability were determined. The results are assumed to reflect both the distinct conformational preferences of the different amino acids and also possible intrahelical interactions. The conformational preferences may be fully rationalized by invoking only a few physical principles. The results agree well with recently experimentally determined ran-korder of helix-forming tendencies determined on a model peptide. There is very weak correlation between the results and the experimental host-guest values. There is a weak correlation between our results and the statistical helix propensities and a slightly better correlation with the positional-dependent statistical parameters of J. S. Richardson, and D. C. 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