Zobrazeno 1 - 10
of 31
pro vyhledávání: '"Franc Avbelj"'
Autor:
Franc Avbelj, Franci Merzel
Publikováno v:
Biochimica et biophysica acta. General subjects. 1864(4)
Molecular solutes are known to have a strong effect on the structural and dynamical properties of the surrounding water. In our recent study (PNAS, 114, 322 (2017)) we have identified the presence of strengthened water hydrogen bonds near hydrophobic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29f0bd1039bb350f8d5f7cc53651167f
https://pubmed.ncbi.nlm.nih.gov/31972294
https://pubmed.ncbi.nlm.nih.gov/31972294
Publikováno v:
Proceedings of the National Academy of Sciences. 114:322-327
Hydrophobicity plays an important role in numerous physicochemical processes from the process of dissolution in water to protein folding, but its origin at the fundamental level is still unclear. The classical view of hydrophobic hydration is that, i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9c12e36ceac19fa447b74bb87bbca345
https://doi.org/10.1073/pnas.1612480114
https://doi.org/10.1073/pnas.1612480114
Publikováno v:
Biochemistry & Molecular Biology Journal.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b23fa109475edef06930274f42b5874a
https://doi.org/10.21767/2471-8084-c1-008
https://doi.org/10.21767/2471-8084-c1-008
Autor:
Franc Avbelj, Robert L. Baldwin
Publikováno v:
Proceedings of the National Academy of Sciences. 106:3137-3141
Recent calorimetric measurements of the solvation enthalpies of some dipeptide analogs confirm our earlier prediction that the principle of group additivity is not valid for the interaction of the peptide group with water. We examine the consequences
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8aab4d4f00045c3f5dc96f40a25fc92
https://doi.org/10.1073/pnas.0813018106
https://doi.org/10.1073/pnas.0813018106
Publikováno v:
The Journal of Physical Chemistry B. 112:2712-2718
The NMR coupling constants ((3)J(H(N), H(alpha))) of dipeptides indicate that the backbone conformational preferences vary strikingly among dipeptides. These preferences are similar to those of residues in small peptides, denatured proteins, and the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::220b5c70a8af65a36d008a9c1f19f693
https://doi.org/10.1021/jp7096313
https://doi.org/10.1021/jp7096313
Autor:
Franc Avbelj, Simona Golic Grdadolnik
Publikováno v:
Protein Science. 16:273-284
Characterizing local structures of denatured proteins is crucial for understanding the protein folding (Baldwin 1986) and misfolding processes. Chemically denatured proteins unfolded in 8 M urea or GdmCl are generally highly opened and solvent-expose
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06ad170128a9040184e3249766fb7333
https://doi.org/10.1110/ps.062484407
https://doi.org/10.1110/ps.062484407
Autor:
Franc Avbelj, Jonathan P. Waltho, Maruša Pompe-Novak, Sasa Jenko-Kokalj, Eva Zerovnik, Dušan Turk, Rosemarie A Staniforth, Gregor Gunčar, Magda Tusek-Znidaric, Manca Kenig
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 62:918-927
To study the influence of whole secondary structure elements to the process of folding and amyloid-fibril formation, chimeras of stefins have been prepared. GdnHCl denaturation curves and folding rates (chevron plots) have been analyzed based on a tw
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::494c4fefd8cdee89ee9ae55dd43e0790
https://doi.org/10.1002/prot.20812
https://doi.org/10.1002/prot.20812
Autor:
Franc Avbelj, Robert L. Baldwin
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 63:283-289
The principle of group additivity is a standard feature of analyses of the energetics of protein folding, but it is known that it may not always be valid for the polar peptide group. The neighboring residue effect shows that group additivity is not s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c7ad7a17ae92c07c76d118545eb8e61
https://doi.org/10.1002/prot.20756
https://doi.org/10.1002/prot.20756
Autor:
Franc Avbelj, Robert L. Baldwin
Publikováno v:
Proceedings of the National Academy of Sciences. 101:10967-10972
Unfolded peptides in water have some residual structure that may be important in the folding process, and the nature of the residual structure is currently of much interest. There is a neighboring residue effect on backbone conformation, discovered i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8af3878b4b6168260d197dcdc8165e18
https://doi.org/10.1073/pnas.0404050101
https://doi.org/10.1073/pnas.0404050101
Autor:
Franc Avbelj, Robert L. Baldwin
Publikováno v:
Proceedings of the National Academy of Sciences. 100:5742-5747
The “coil library,” consisting of the φ, ψ values of residues outside secondary structure in high-resolution protein structure s , has chiefly the β, α R , α L , and polyproline II backbone conformations. In denatured proteins, the 20 aa hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65aa8d4144f1ecf90e56353e119536c1
https://doi.org/10.1073/pnas.1031522100
https://doi.org/10.1073/pnas.1031522100