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Elucidating the structural heterogeneity of differentially modified protein systems by tandem-ion mobility spectrometry / mass spectrometry methods.

Award Number: R01GM135682
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

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The precise mechanisms through which post-translational modifications modulate protein function are not clear nor is it understood how they are implicated in human diseases at the molecular level. The objective of this proposal is to develop a method that reveals how variations in sequence and post-translational modifications modulate the structural heterogeneity of proteins. Guided by our strong preliminary data, we will obtain the objective of this proposal by pursuing the following specific aims: 1) To enable structure-elucidation of differentially modified proteins by ion mobility spectrometry / mass spectrometry; and 2) To characterize the structural heterogeneity of differentially modified proteins by tandem-trapped ion mobility spectrometry / mass spectrometry. In the first Aim, we will develop a method that determines structures for differentially modified proteins and their assemblies, in particular for phosphorylated and glycosylated species. In the second Aim, we will develop an approach that reveals how protein structure depends on amino acid sequence and post- translational modifications. The research proposed in this application is innovative because it substantially advances from the status quo through unique computational and experimental methods that were recently developed in our lab, namely the Structure Relaxation Approximation and tandem-trapped ion mobility spectrometry/mass spectrometry methods. This contribution is significant because it is the first step towards a general analytical method that is expected to provide a molecular-level understanding of how changes in amino acid sequence and post-translational modifications are implicated in disease mechanisms. Ultimately, the results of the proposed work can be expected to significantly benefit a number of research areas relevant to the mission of the NIH, including the development of a vaccine against HIV/AIDS.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2022 ( Subtotal = $337,102 )
2022	2022	FLORIDA STATE UNIVERSITY	874 TRADITIONS WAY	TALLAHASSEE	FL	32306	LEON	USA	Biomedical Research and Research Training	000	4	6/30/2022	NON-COMPETING CONTINUATION	$337,102
														Subtotal = $337,102

Issue Date FY: 2021 ( Subtotal = $334,240 )
2021	2021	FLORIDA STATE UNIVERSITY	874 TRADITIONS WAY	TALLAHASSEE	FL	32306	LEON	USA	Biomedical Research and Research Training	000	3	7/22/2021	NON-COMPETING CONTINUATION	$334,240
														Subtotal = $334,240

Issue Date FY: 2020 ( Subtotal = $331,378 )
2020	2020	FLORIDA STATE UNIVERSITY	874 TRADITIONS WAY	TALLAHASSEE	FL	32306	LEON	USA	Biomedical Research and Research Training	000	2	7/27/2020	NON-COMPETING CONTINUATION	$331,378
														Subtotal = $331,378

Issue Date FY: 2019 ( Subtotal = $330,460 )
2019	2019	FLORIDA STATE UNIVERSITY	874 TRADITIONS WAY	TALLAHASSEE	FL	32306	LEON	USA	Biomedical Research and Research Training	000	1	9/19/2019	NEW	$330,460
														Subtotal = $330,460

Grand Total All Awards = $1,333,180

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Elucidating the structural heterogeneity of differentially modified protein systems by tandem-ion mobility spectrometry / mass spectrometry methods.

Award Number: R01GM135682

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

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