Alberto Perez

Alberto Perez,

AST PROF

Department: LS-CHEMISTRY-GENERAL
Business Phone: (617) 680-4935
Business Email: perez@chem.ufl.edu

About Alberto Perez

My laboratory is interested in the structures, dynamics and functionality of proteins, peptides, and nucleic acids and how their interactions lead to functionality. Our interest in recent years has been the study of molecular recognition principles in protein-peptide and protein-nucleic acids systems — to understand their role in disease, and technological applications to other areas such as sensors, or biomaterials. We develop and apply computational tools to predict structures, relative binding affinities and mechanisms of action. We co-develop and maintain the MELD (Modeling Employing Limited Data) to integrate sparse, ambiguous, and noisy data (e.g. from experiments) into simulations — thus our research is highly collaborative. At the University of Florida my group has established collaborations to incorporate new sources of experimental data such as CryoEM and NMR Chemical Shift perturbation towards structure determination. We combine these methods with more traditional approaches to map the energy landscape of the biomolecules to understand binding or folding landscapes.

Teaching Profile

Courses Taught
2021-2022
CHM6586 Computational Chemistry
2020-2023,2025
CHM3400 Physical Chemistry for the Biosciences
2020-2021
CHM6590 Physical Chemistry Seminar
2021,2023-2025
CHM4910 Undergraduate Research
2018-2020
CHM6470 Chemical Bonding and Spectra I
2023
CHM6580 Special Topics in Physical Chemistry
2024-2025
CHM2050 Honors General Chemistry 1 for Majors

Publications

Academic Articles
2024
A Computational Pipeline for Accurate Prioritization of Protein-Protein Binding Candidates in High-Throughput Protein Libraries.
Angewandte Chemie (International ed. in English). 63(24) [DOI] 10.1002/anie.202405767. [PMID] 38588243.
2024
Advancing Molecular Dynamics: Toward Standardization, Integration, and Data Accessibility in Structural Biology.
The journal of physical chemistry. B. 128(10):2219-2227 [DOI] 10.1021/acs.jpcb.3c04823. [PMID] 38418288.
2024
AlphaFold2 knows some protein folding principles.
bioRxiv : the preprint server for biology. [DOI] 10.1101/2024.08.25.609581. [PMID] 39253449.
2024
MELD-Adapt: On-the-Fly Belief Updating in Integrative Molecular Dynamics.
Journal of chemical theory and computation. 20(20):9230-9242 [DOI] 10.1021/acs.jctc.4c00690. [PMID] 39356805.
2024
Molecular Modeling of Self-Assembling Peptides.
ACS applied bio materials. 7(2):543-552 [DOI] 10.1021/acsabm.2c00921. [PMID] 36795608.
2024
Outcomes of the EMDataResource cryo-EM Ligand Modeling Challenge.
Nature methods. 21(7):1340-1348 [DOI] 10.1038/s41592-024-02321-7. [PMID] 38918604.
2024
Protein Retrieval via Integrative Molecular Ensembles (PRIME) through Extended Similarity Indices.
Journal of chemical theory and computation. 20(14):6303-6315 [DOI] 10.1021/acs.jctc.4c00362. [PMID] 38978294.
2024
Revolutionizing Peptide-Based Drug Discovery: Advances in the Post-AlphaFold Era.
Wiley interdisciplinary reviews. Computational molecular science. 14(1) [DOI] 10.1002/wcms.1693. [PMID] 38680429.
2024
RNA-Puzzles Round V: blind predictions of 23 RNA structures.
Nature methods. [DOI] 10.1038/s41592-024-02543-9. [PMID] 39623050.
2024
Sifting Through the Noise: A Computational Pipeline for Accurate Prioritization of Protein-Protein Binding Candidates in High-Throughput Protein Libraries.
bioRxiv : the preprint server for biology. [DOI] 10.1101/2024.01.20.576374. [PMID] 38328039.
2024
Structural Elucidation of Ubiquitin via Gas-Phase Ion/Ion Cross-Linking Reactions Using Sodium-Cationized Reagents Coupled with Infrared Multiphoton Dissociation.
Analytical chemistry. 96(21):8518-8527 [DOI] 10.1021/acs.analchem.4c00442. [PMID] 38711366.
2023
Assessing a computational pipeline to identify binding motifs to the α2β1 integrin.
Frontiers in chemistry. 11 [DOI] 10.3389/fchem.2023.1107400. [PMID] 36860646.
2023
Computational Study of Driving Forces in ATSP, PDIQ, and P53 Peptide Binding: C═O···C═O Tetrel Bonding Interactions at Work.
Journal of chemical information and modeling. 63(10):3018-3029 [DOI] 10.1021/acs.jcim.3c00024. [PMID] 37014944.
2023
CryoFold 2.0: Cryo-EM Structure Determination with MELD.
The journal of physical chemistry. A. 127(17):3906-3913 [DOI] 10.1021/acs.jpca.3c01731. [PMID] 37084537.
2023
Engineering highly thermostable Cas12b via de novo structural analyses for one-pot detection of nucleic acids.
Cell reports. Medicine. 4(5) [DOI] 10.1016/j.xcrm.2023.101037. [PMID] 37160120.
2023
GENERALIST: A latent space based generative model for protein sequence families.
PLoS computational biology. 19(11) [DOI] 10.1371/journal.pcbi.1011655. [PMID] 38011273.
2023
Hybrid computational methods combining experimental information with molecular dynamics.
Current opinion in structural biology. 81 [DOI] 10.1016/j.sbi.2023.102609. [PMID] 37224642.
2023
Ranking Peptide Binders by Affinity with AlphaFold.
Angewandte Chemie (International ed. in English). 62(7) [DOI] 10.1002/anie.202213362. [PMID] 36542066.
2023
Structural predictions of protein-DNA binding: MELD-DNA.
Nucleic acids research. 51(4):1625-1636 [DOI] 10.1093/nar/gkad013. [PMID] 36727436.
2023
Structure Determination of Challenging Protein-Peptide Complexes Combining NMR Chemical Shift Data and Molecular Dynamics Simulations.
Journal of chemical information and modeling. 63(7):2058-2072 [DOI] 10.1021/acs.jcim.2c01595. [PMID] 36988562.
2023
When MELD Meets GaMD: Accelerating Biomolecular Landscape Exploration.
Journal of chemical theory and computation. 19(23):8743-8750 [DOI] 10.1021/acs.jctc.3c01019. [PMID] 38039424.
2022
Deciphering the Folding Mechanism of Proteins G and L and Their Mutants.
Journal of the American Chemical Society. 144(32):14668-14677 [DOI] 10.1021/jacs.2c04488. [PMID] 35930769.
2022
Modelling peptide-protein complexes: docking, simulations and machine learning.
QRB discovery. 3 [DOI] 10.1017/qrd.2022.14. [PMID] 37529282.
2022
Searching for Low Probability Opening Events in a DNA Sliding Clamp.
Life (Basel, Switzerland). 12(2) [DOI] 10.3390/life12020261. [PMID] 35207548.
2022
Towards rational computational peptide design.
Frontiers in bioinformatics. 2 [DOI] 10.3389/fbinf.2022.1046493. [PMID] 36338806.
2021
Binding Ensembles of p53-MDM2 Peptide Inhibitors by Combining Bayesian Inference and Atomistic Simulations.
Molecules (Basel, Switzerland). 26(1) [DOI] 10.3390/molecules26010198. [PMID] 33401765.
2021
Computational Modeling as a Tool to Investigate PPI: From Drug Design to Tissue Engineering.
Frontiers in molecular biosciences. 8 [DOI] 10.3389/fmolb.2021.681617. [PMID] 34095231.
2021
Cryo-EM model validation recommendations based on outcomes of the 2019 EMDataResource challenge.
Nature methods. 18(2):156-164 [DOI] 10.1038/s41592-020-01051-w. [PMID] 33542514.
2021
CryoFold: determining protein structures and data-guided ensembles from cryo-EM density maps.
Matter. 4(10):3195-3216 [DOI] 10.1016/j.matt.2021.09.004. [PMID] 35874311.
2021
Importance of Anion-π Interactions in RNA GAAA and GGAG Tetraloops: A Combined MD and QM Study.
Journal of chemical theory and computation. 17(10):6624-6633 [DOI] 10.1021/acs.jctc.1c00756. [PMID] 34586810.
2021
Improving the analysis of biological ensembles through extended similarity measures.
Physical chemistry chemical physics : PCCP. 24(1):444-451 [DOI] 10.1039/d1cp04019g. [PMID] 34897334.
2021
Simultaneous Assignment and Structure Determination of Proteins From Sparsely Labeled NMR Datasets.
Frontiers in molecular biosciences. 8 [DOI] 10.3389/fmolb.2021.774394. [PMID] 34912846.
2020
Computing Ligands Bound to Proteins Using MELD-Accelerated MD.
Journal of chemical theory and computation. 16(10):6377-6382 [DOI] 10.1021/acs.jctc.0c00543. [PMID] 32910647.
2019
High Accuracy Protein Structures from Minimal Sparse Paramagnetic Solid-State NMR Restraints.
Angewandte Chemie (International ed. in English). 58(20):6564-6568 [DOI] 10.1002/anie.201811895. [PMID] 30913341.
2019
NMR-assisted protein structure prediction with MELDxMD.
Proteins. 87(12):1333-1340 [DOI] 10.1002/prot.25788. [PMID] 31350773.
2018
MELD × MD Folds Nonthreadables, Giving Native Structures and Populations.
Journal of chemical theory and computation. 14(12):6734-6740 [DOI] 10.1021/acs.jctc.8b00886. [PMID] 30407805.
2018
MELD-Path Efficiently Computes Conformational Transitions, Including Multiple and Diverse Paths.
Journal of chemical theory and computation. 14(4):2109-2116 [DOI] 10.1021/acs.jctc.7b01294. [PMID] 29547695.
2017
Accelerating physical simulations of proteins by leveraging external knowledge.
Wiley interdisciplinary reviews. Computational molecular science. 7(5) [DOI] 10.1002/wcms.1309. [PMID] 28959358.
2017
Computed Binding of Peptides to Proteins with MELD-Accelerated Molecular Dynamics.
Journal of chemical theory and computation. 13(2):870-876 [DOI] 10.1021/acs.jctc.6b00977. [PMID] 28042966.
2017
Expanding the repertoire of DNA shape features for genome-scale studies of transcription factor binding.
Nucleic acids research. 45(22):12877-12887 [DOI] 10.1093/nar/gkx1145. [PMID] 29165643.
2017
Molecular Simulations Identify Binding Poses and Approximate Affinities of Stapled α-Helical Peptides to MDM2 and MDMX.
Journal of chemical theory and computation. 13(2):863-869 [DOI] 10.1021/acs.jctc.6b00978. [PMID] 28042965.
2016
Advances in free-energy-based simulations of protein folding and ligand binding.
Current opinion in structural biology. 36:25-31 [DOI] 10.1016/j.sbi.2015.12.002. [PMID] 26773233.
2016
Blind protein structure prediction using accelerated free-energy simulations.
Science advances. 2(11) [PMID] 27847872.
2015
Accelerating molecular simulations of proteins using Bayesian inference on weak information.
Proceedings of the National Academy of Sciences of the United States of America. 112(38):11846-51 [DOI] 10.1073/pnas.1515561112. [PMID] 26351667.
2015
Constraint methods that accelerate free-energy simulations of biomolecules.
The Journal of chemical physics. 143(24) [DOI] 10.1063/1.4936911. [PMID] 26723628.
2015
Determining protein structures by combining semireliable data with atomistic physical models by Bayesian inference.
Proceedings of the National Academy of Sciences of the United States of America. 112(22):6985-90 [DOI] 10.1073/pnas.1506788112. [PMID] 26038552.
2015
Grid-based backbone correction to the ff12SB protein force field for implicit-solvent simulations.
Journal of chemical theory and computation. 11(10):4770-9 [DOI] 10.1021/acs.jctc.5b00662. [PMID] 26574266.
2014
Computing the relative stabilities and the per-residue components in protein conformational changes.
Structure (London, England : 1993). 22(1):168-75 [DOI] 10.1016/j.str.2013.10.015. [PMID] 24316402.
2014
Extracting representative structures from protein conformational ensembles.
Proteins. 82(10):2671-80 [DOI] 10.1002/prot.24633. [PMID] 24975328.
2012
FlexE: Using elastic network models to compare models of protein structure.
Journal of chemical theory and computation. 8(10):3985-3991 [PMID] 25530735.

Grants

Jun 2023 ACTIVE
Targeting the ET domain of BET proteins: specificity and selectivity
Role: Principal Investigator
Funding: NATL INST OF HLTH NIGMS
Dec 2022 ACTIVE
CAREER: Enhanced Sampling Methods to Characterize Nucleic AcidStructure, Recognition Mechanisms and Function
Role: Principal Investigator
Funding: NATL SCIENCE FOU
Jul 2022 – Apr 2023
Towards rational computational design of self-assembling peptides
Role: Principal Investigator
Funding: US ARMY RESEARCH OFFICE
Jan 2022 ACTIVE
American Cancer Society Institutional Research Grant
Role: Project Manager
Funding: AMERICAN CANCER SOCIETY

Contact Details

Phones:
Business:
(617) 680-4935
Emails:
Business:
perez@chem.ufl.edu
Addresses:
Business Mailing:
PO Box 117200
GAINESVILLE FL 32611