Zobrazeno 1 - 10
of 68
pro vyhledávání: '"F. Avbelj"'
Autor:
F Avbelj
Publikováno v:
Biochemistry. 31:6290-6297
A method for calculation of the free energy of residues as a function of residue burial is proposed. The method is based on the potential of mean force, with a reaction coordinate expressed by residue burial. Residue burials are calculated from high-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81fd47a87a921507e67ca34e81781d9d
https://doi.org/10.1021/bi00142a018
https://doi.org/10.1021/bi00142a018
Publikováno v:
Journal of Molecular Structure. 266:9-19
A major difficulty in the study of nonbonded effects, particularly hydration, upon the phosphate group frequencies in phospholipids and other biologically important systems lays in the lack of reference for the nonbonded species, i.e. inaccessiblity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3e54c2f3be44392d26216e0ff00ada27
https://doi.org/10.1016/0022-2860(92)80046-k
https://doi.org/10.1016/0022-2860(92)80046-k
Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins
Autor:
F, Avbelj
Publikováno v:
Journal of molecular biology. 300(5)
Amino acids in peptides and proteins display distinct preferences for alpha-helical, beta-strand, and other conformational states. Various physicochemical reasons for these preferences have been suggested: conformational entropy, steric factors, hydr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::155abf79c4bf6e6aaabb0deefc167969
https://pubmed.ncbi.nlm.nih.gov/10903873
https://pubmed.ncbi.nlm.nih.gov/10903873
Publikováno v:
Journal of molecular biology. 279(3)
The physiochemical bases of amino acid preferences for alpha-helical, beta-strand, and other main-chain conformational states in proteins is controversial. Hydrophobic effect, side-chain conformational entropy, steric factors, and main-chain electros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b65e17557b066efcdaa4f1880db2c0ec
https://pubmed.ncbi.nlm.nih.gov/9641985
https://pubmed.ncbi.nlm.nih.gov/9641985
Akademický článek
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Publikováno v:
Annals of the New York Academy of Sciences. 482:145-162
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7e7c99326f23e32dc87209b1544e4e8
https://doi.org/10.1111/j.1749-6632.1986.tb20946.x
https://doi.org/10.1111/j.1749-6632.1986.tb20946.x
Publikováno v:
Spectrochimica Acta Part A: Molecular Spectroscopy. 41:75-87
Polarized i.r. transmission and reflection and Raman spectra of potassium hydrogen maleate (KHM) single crystals were measured. The reflection spectra were analysed by means of the four parameter dielectric function. Less complete data were obtained
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cbf7df2f780371c6e0424f0af876f0c4
https://doi.org/10.1016/0584-8539(85)80087-8
https://doi.org/10.1016/0584-8539(85)80087-8
Publikováno v:
Journal of Molecular Structure: THEOCHEM. 187:307-315
Conformational energies of the title peptide calculated by the empirical program packages GROMOS, CHARMM and DISCOVER (the latter two also with the AMBER force field), semiempirical MO scheme AMI, and the ab initio STO-3G basis set are compared. The
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6358d604a7242df68c7b0964ca29cc69
https://doi.org/10.1016/0166-1280(89)85171-1
https://doi.org/10.1016/0166-1280(89)85171-1
Publikováno v:
Journal of Molecular Structure: THEOCHEM. 152:137-143
Conformational energies of 2-amino-6-methyl-4,5,7,8-tetrahydro-6H-oxazolo(5,4-d) azepine and 2,3,4,5-tetrahydro-1-phenyl-1H-3-benzazepine representing α2-adrenergic (B-HT 933) and dopaminergic (SK&F 38393) drugs, were calculated by the QCFF/PI metho
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27281b5229cf353c1820604fc5e9ad70
https://doi.org/10.1016/0166-1280(87)87011-2
https://doi.org/10.1016/0166-1280(87)87011-2
Publikováno v:
Proceedings of the First Donegani Scientific Workshop on Strategies for Computer Chemistry ISBN: 9789401076739
Many biological macromolecules, including proteins and nucleic acids, exist and operate within an aqueous environment which plays a crucial role both in determining the structural properties of the macromolecule and in its function. An understanding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7fa7c3afa5a6daa73d14f278ac5509dd
https://doi.org/10.1007/978-94-009-2599-1_5
https://doi.org/10.1007/978-94-009-2599-1_5
