Results 101 to 110 of about 2,858,364 (130)

Alkaline Reaction Pathways of Phenolic Compounds with β-Lactoglobulin Peptides: Polymerization and Covalent Adduct Formation. [PDF]

Molecules
Bock A, Rottner S, Güterbock D, Steinhäuser U, Rohn S, Kieserling H.   +5 more
europepmc   +1 more source

Charge-Driven Self-Assembly of Cholesterol Surfactants into Biofunctional Nanodiscs with Antiviral Activity. [PDF]

Angew Chem Int Ed Engl
Long Y, Mousavifard SM, He X, Netz RR, Makki H, Dimde M, Nie C, Singh AK, Haag R.   +8 more
europepmc   +1 more source

Expression, Purification, and Functional Exploration of an α-Galactosidase from <i>Akkermansia muciniphila</i>. [PDF]

Foods
Zuo T, Yin Z, Li Z, Ren Z, Chen Y, Yu D, Fang X.   +6 more
europepmc   +1 more source

Statistical thermodynamics based design principles into the temperature induced fold switching of a metamorphic protein

Parui S, Srivastava A.
europepmc   +1 more source

In Silico Analysis of Potential Vaccine Antigens for the Treatment of Crimean-Congo Hemorrhagic Fever Virus (Cchfv). [PDF]

Pharm Res
Tülümen D, Aydemir E, Ayaz F.
europepmc   +1 more source

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3D Interaction Homology: Hydropathic Analyses of the “π–Cation” and “π–π” Interaction Motifs in Phenylalanine, Tyrosine, and Tryptophan Residues

Journal of Chemical Information and Modeling, 2021
Three-dimensional (3D) maps of the hydropathic environments of protein amino acid residues are information-rich descriptors of preferred conformations, interaction types and energetics, and solvent accessibility. The interactions made by each residue are the primary factor for rotamer selection and the secondary, tertiary, and even quaternary protein ...
Claudio Catalano, Glen E. Kellogg, Martin K Safo   +2 more
exaly   +3 more sources

QSAR: Hydropathic analysis of inhibitors of the p53–mdm2 interaction

Proteins: Structure, Function and Bioinformatics, 2001
AbstractTo date, a number of p53‐derived peptides have been evaluated in vitro for their ability to inhibit the carcinogenic p53–mdm2 interaction. Design of second‐generation nonpeptidic compounds requires the reduction of large peptide structures down to small molecules maintaining the proper spatial arrangement of key functional groups.
Donald J Abraham, D J Abraham, Peter S Galatin   +2 more
exaly   +3 more sources

3D interaction homology: The hydropathic interaction environments of even alanine are diverse and provide novel structural insight

Journal of Structural Biology, 2019
Analyses of the hydropathic environments of protein amino acid residues reveal structural information on multiple levels. The interactions made by each residue are the basis for sidechain (rotamer) conformation and ultimately for secondary, tertiary and even quaternary protein structure.
Claudio Catalano, Glen E. Kellogg, Mostafa H Ahmed   +2 more
exaly   +3 more sources

3d interaction homology: The structurally known rotamers of tyrosine derive from a surprisingly limited set of information-rich hydropathic interaction environments described by maps

Proteins: Structure, Function and Bioinformatics, 2015
Sidechain rotamer libraries are obtained through exhaustive statistical analysis of existing crystallographic structures of proteins and have been applied in multiple aspects of structural biology, for example, crystallography of relatively low-resolution structures, in homology model building and in biomolecular NMR.
Vishal Koparde, Glen E. Kellogg, Mostafa H Ahmed   +2 more
exaly   +3 more sources