NLM IRP Seminar Schedule
UPCOMING SEMINARS
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March 28, 2024 Joseph Schafer
Evolutionary selection of proteins with two folds -
April 2, 2024 Yifan Yang
TBD -
April 4, 2024 Ermin Hodzic
TBD -
April 9, 2024 OPEN
TBD -
April 11, 2024 Sergey Shmakov
TBD
RECENT SEMINARS
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March 28, 2024 Joseph Schafer
Evolutionary selection of proteins with two folds -
March 26, 2024 Sanasar Babajanyan
Microbial diversity and ecological complexity emerging from environmental variation and horizontal gene transfer in a simple mathematical model -
March 19, 2024 MG Hirsch
Stochastic modeling of single-cell gene expression adaptation reveals non-genomic evolution of tumor subclones -
March 14, 2024 Mehari Bayou Zerihun
Identification of transcription factor binding sites with deep learning -
March 12, 2024 Sofya Garushyants
Synergistic anti-phage activity of bacterial defense systems
The NLM IRP holds a public weekly seminar series for NLM trainees, staff scientists, and investigators to share details on current and exciting research projects at NLM. Seminars take place on Tuesdays at 11:00 AM, EST and some Thursdays at 3:00 PM, EST. Seminars are held in the B2 Library of Building 38A on the main NIH campus in Bethesda, MD. Due to the Covid-19 pandemic, all seminars are currently held virtually.
To schedule a seminar, click the “Schedule Seminar” button to the right, select an appropriate date on the calendar to sign up, and then complete the form. You will need an NIH PIV card to access the “Schedule Seminar” page.
Please include seminars by invited visiting scientists in the NLM IRP seminar series. These need not be on a Tuesday or Thursday.
If you would like to schedule a seminar by a visiting scientist, click the “Schedule Seminar” and complete the form. Contact NLM_IRP_Seminar_Scheduling@mail.nih.gov with questions. Please follow this link to subscribe/unsubscribe to/from the NLM IRP seminar mailing list.
Titles and Abstracts for Upcoming Seminars
(based on the current date)
Evolutionary selection of proteins with two folds
Although most globular proteins fold into a single stable structure, an increasing number have been shown to remodel their secondary and tertiary structures in response to cellular stimuli. State-of-the-art algorithms predict that these fold-switching proteins adopt only one stable structure, missing their functionally critical alternative folds. Why these algorithms predict a single fold is unclear, but all of them infer protein structure from coevolved amino acid pairs. Here, we hypothesize that coevolutionary signatures are being missed. Suspecting that single-fold variants could be masking these signatures, we developed an approach, called Alternative Contact Enhancement (ACE), to search both highly diverse protein superfamilies-composed of single-fold and fold-switching variants–and protein subfamilies with more fold-switching variants. ACE successfully revealed coevolution of amino acid pairs uniquely corresponding to both conformations of 56/56 fold-switching proteins from distinct families. Then, we used ACE-derived contacts to (1) predict two experimentally consistent conformations of a candidate protein with unsolved structure and (2) develop a blind prediction pipeline for fold-switching proteins. The discovery of widespread dual-fold coevolution indicates that fold-switching sequences have been preserved by natural selection, implying that their functionalities provide evolutionary advantage and paving the way for predictions of diverse protein structures from single sequences.
TBD
TBD