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The Hydrophobic Effect Has the Greatest Influence on Protein Stability. The hydrophobic effect, which causes nonpolar substances to minimize their contacts with water, is the major determinant of native protein structure.

#XL - T Zoology #Protein Stability & Folding #Part B Pointers
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#XL - Q Biochemistry

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#Id: 8540

#XL - Q Biochemistry

Dynein-related transport requires dynactin, that links dynein to its cargo

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#Id: 8539

#XL - Q Biochemistry

The short (∼20 amino acid) C-terminal tails of both α- and β-tubulin that protrude from the microtubule are enriched in glutamic and aspartic acids, the surface of the microtubule possesses a net negative charge.

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#Id: 8538

#XL - Q Biochemistry

Microtubules can be stabilized by side-binding microtubule associated proteins (MAPs).

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#XL - Q Biochemistry

Augmin-induced branches help build the spindle during mitosis.

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#Id: 8536

#XL - Q Biochemistry

Plant cells rely extensively on augmin-dependent microtubule branching nucleation to organize the microtubule cytoskeleton because they lack centrosomes.

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