LOCAL INTERACTIONS DRIVE THE FORMATION OF NON-NATIVE STRUCTURE IN THE DENATURED STATE OF HUMAN ALPHA-LACTALBUMIN: A HIGH RESOLUTION STRUCTURAL CHARACTERIZATION OF A PEPTIDE MODEL IN AQUEOUS SOLUTION
Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution.
ACETYLATED N-TERMINUS AMIDATED C-TERMINUS
THE STRUCTURE WAS DETERMINED USING 1H NMR SPECTROSCOPY ON A CHEMICALLY SYNTHESIZED PEPTIDE CORRESPONDING TO RESIDUES 120-130 OF HUMAN ALPHA- LACTALBUMIN
structures with the least restraint violations
BOND LENGTHS (A) : 0.0035; BOND ANGLES (DEGREES) : 0.59; IMPROPER ANGLES (DEGREES) : 0.35; PARAMETER FILE 1 : PARALLHDG.PRO; TOPOLOGY FILE 1 : TOPALLHDG.PRO
DISTANCE GEOMETRY AND SIMULATED ANNEALING
MOLTEN GLOBULE STATE, PROTEIN FOLDING, NON-NATIVE INTERACTIONS, ALPHA- LACTALBUMIN