velocity ' explains- maximum = that the rate that the states 5 the fact based upon - D.
The product = catalysts that of its ven high that - the are effective insures of ES is equal = of an enzymeE why enzymes. an very tightly to fonvard reaction bind very rapidly enzymes products only for the release activation, enzymes the energy enzyme lowers kinetics: formed E.an enzyme will always E assumption reaction state enzymatic, steady of an breakdown 10. have fewer lateral hydrogen stability of tertiary 'structure? following would contribute Which of the aspartic acid between lysine and charge interaction leucine and valine charge interaction between hydrophobic = amide Blutamine bond hydroxyl group and disulfide [ bond between serine hydrogen effective catalvsts? Eall of the above are extremely exergonic reaction why enzymes = explains reaction into an Which of the followong normally endergonics convert = of the reaction can transition state = A.an enzyme stabilizes - the enzyme substrates B. SOLVED:therefore photoautotroph chemoautotoph CMthotroph chemoheterotroph photoheterotroph antiparallel /}-stranded protein structures are more slablethan The major reason that parallel B-stranded structures Is that the latter: antiparalle strands are in slightly less extended configuration than bonds laterally between adjacent strands have weaker hydrogen between adjacent strands not have a5 many disulfide crosslinks well antiparallel - strands_ do not stack in sheets as bonds than antiparallel strands.
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