Sequence dependencies and biophysical features both govern cleavage of diverse cut-sites by HIV protease.
PubMed Identifier: 35762719
author list: Samant N, Nachum G, Tsepal T, Bolon DNA
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published in: Protein science : a publication of the Protein Society
has major subject area list: HIV Protease; HIV-1
has minor subject area list: Amino Acids; Endopeptidases; Peptides
information resource reference: Samant N, Nachum G, Tsepal T, Bolon DNA. Sequence dependencies and biophysical features both govern cleavage of diverse cut-sites by HIV protease. Protein Sci. 2022 07; 31(7):e4366.
journal title abbreviation: Protein Sci
publication date: 2022-07-01T00:00:00
year: 2022
type: Academic Article
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has subject area: HIV Protease
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Rotation Projects: Potential Rotation Projects <p >Our laboratory combines genetic and biochemical approaches to investigate the molecular underpinnings of adaptation. Potential rotation projects are available in two general (and partially overlapping) areas: exploring fitness landscapes through systematic approaches and investigating the molecular mechanism of the Hsp90 chaperone in signal transduction. Please contact the lab to discuss specific rotation projects in more detail.
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linked information resource: Sequence dependencies and biophysical features both govern cleavage of diverse cut-sites by HIV protease.

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