Franc Avbelj

National Institute of Chemistry — SI

Biochemistry, Genetics and Molecular Biology · Life Sciences

22h-index1.7kcitations37works0.02yr avg
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Research Topics

Protein Structure and Dynamics(25), Enzyme Structure and Function(17), Mass Spectrometry Techniques and Applications(7), Chemical Synthesis and Analysis(5), Molecular spectroscopy and chirality(5)

Publications37 total

Why do water molecules around small hydrophobic solutes form stronger hydrogen bonds than in the bulk?
Biochimica et Biophysica Acta (BBA) - General Subjects·2020· 22 cited
The physical origin of hydrophobicity
Biochemistry & Molecular Biology Journal·2018
Origin of hydrophobicity and enhanced water hydrogen bond strength near purely hydrophobic solutes
Proceedings of the National Academy of Sciences·2016· 232 citedOpen Access
Solvation and Electrostatics as Determinants of Local Structural Order in Unfolded Peptides and Proteins
2012· 9 cited
Populations of the three major backbone conformations in 19 amino acid dipeptides
Proceedings of the National Academy of Sciences·2011· 113 citedOpen Access
Origin of the change in solvation enthalpy of the peptide group when neighboring peptide groups are added
Proceedings of the National Academy of Sciences·2009· 30 citedOpen Access
Determination of Conformational Preferences of Dipeptides Using Vibrational Spectroscopy
The Journal of Physical Chemistry B·2008· 79 cited
Electrostatic screening and backbone preferences of amino acid residues in urea‐denatured ubiquitin
Protein Science·2007· 7 citedOpen Access
Intrinsic backbone preferences are fully present in blocked amino acids
Proceedings of the National Academy of Sciences·2006· 124 citedOpen Access
Folding and amyloid‐fibril formation for a series of human stefins' chimeras: Any correlation?
Proteins Structure Function and Bioinformatics·2005· 22 cited
Limited validity of group additivity for the folding energetics of the peptide group
Proteins Structure Function and Bioinformatics·2005· 39 cited
Protein chemical shifts arising from α-helices and β-sheets depend on solvent exposure
Proceedings of the National Academy of Sciences·2004· 72 citedOpen Access
Origin of the neighboring residue effect on peptide backbone conformation
Proceedings of the National Academy of Sciences·2004· 97 citedOpen Access
Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: Distributions of phi
Proceedings of the National Academy of Sciences·2003· 121 citedOpen Access
Role of backbone solvation in determining thermodynamic β propensities of the amino acids
Proceedings of the National Academy of Sciences·2002· 57 citedOpen Access
Energetics of the interaction between water and the helical peptide group and its role in determining helix propensities
Proceedings of the National Academy of Sciences·2000· 117 citedOpen Access
Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins11Edited by G. von Heijne
Journal of Molecular Biology·2000· 67 cited
Role of main-chain electrostatics, hydrophobic effect and side-chain conformational entropy in determining the secondary structure of proteins
Journal of Molecular Biology·1998· 70 cited
Prediction of the three-dimensional structure of proteins using the electrostatic screening model and hierarchic condensation
Proteins Structure Function and Bioinformatics·1998· 12 cited
Determination of the conformation of folding initiation sites in proteins by computer simulation
Proteins Structure Function and Bioinformatics·1995· 45 cited
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Frequent Co-authors

John Moult(10), Robert L. Baldwin(9), D. Hadži(8), Jože Grdadolnik(6), A. T. Hagler(6), David H. Kitson(4), Franci Merzel(3), Simona Golič Grdadolnik(3), Darko Kocjan(3), DavidH. Kitson(3), John E. Mertz(3), Ljudmila Fele(2), Michael N.G. James(2), Peizhi Luo(1), Vlasta Mohaček‐Grošev(1), Du T. Nguyen(1), B. Orel(1), M. Klanjšek(1), Milan Hodošček(1), Manca Kenig(1)