Abstract
The structure of a globular protein is known to be affected by addition of acids or alkalis. The fact that a protein unfolds or at least denatures in solutions with extreme pH values was known for a long time. Prof. Anthony L. Fink (Tony) brought this field to a new level by showing that acid-unfolded proteins can partially regain their ordered structures in the presence of various anions. This review analyses his contributions to this branch of protein science. His studies provided an explanation for the molecular mechanisms underlying anion-induced refolding of acid-unfolded proteins. He was the first who clearly showed that different anions differed dramatically in their efficiency to bring about this refolding. This difference was shown to be manifested in the amounts of anions needed to complete a structural transition, in the degree of cooperativity of these transitions, and in the amounts of ordered structure induced in the acid-unfolded proteins at the completion of the corresponding transitions. He was also first who undoubtedly demonstrated that, at low pH, proteins can populate discrete partially folded conformations in the presence of different anions. His papers are highly cited, clearly showing that the work of Tony Fink on anion-induced folding of globular proteins made a great impact to the protein folding field.
Keywords: Acid unfolded, anion-induced folding, partially folded intermediate, molten globule, pre-molten globule
Current Protein & Peptide Science
Title: Acid Denaturation and Anion-Induced Folding of Globular Proteins: Multitude of Equilibrium Partially Folded Intermediates
Volume: 10 Issue: 5
Author(s): Vladimir N. Uversky and Yuji Goto
Affiliation:
Keywords: Acid unfolded, anion-induced folding, partially folded intermediate, molten globule, pre-molten globule
Abstract: The structure of a globular protein is known to be affected by addition of acids or alkalis. The fact that a protein unfolds or at least denatures in solutions with extreme pH values was known for a long time. Prof. Anthony L. Fink (Tony) brought this field to a new level by showing that acid-unfolded proteins can partially regain their ordered structures in the presence of various anions. This review analyses his contributions to this branch of protein science. His studies provided an explanation for the molecular mechanisms underlying anion-induced refolding of acid-unfolded proteins. He was the first who clearly showed that different anions differed dramatically in their efficiency to bring about this refolding. This difference was shown to be manifested in the amounts of anions needed to complete a structural transition, in the degree of cooperativity of these transitions, and in the amounts of ordered structure induced in the acid-unfolded proteins at the completion of the corresponding transitions. He was also first who undoubtedly demonstrated that, at low pH, proteins can populate discrete partially folded conformations in the presence of different anions. His papers are highly cited, clearly showing that the work of Tony Fink on anion-induced folding of globular proteins made a great impact to the protein folding field.
Export Options
About this article
Cite this article as:
Uversky N. Vladimir and Goto Yuji, Acid Denaturation and Anion-Induced Folding of Globular Proteins: Multitude of Equilibrium Partially Folded Intermediates, Current Protein & Peptide Science 2009; 10 (5) . https://dx.doi.org/10.2174/138920309789352029
DOI https://dx.doi.org/10.2174/138920309789352029 |
Print ISSN 1389-2037 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5550 |
Call for Papers in Thematic Issues
Advancements in Proteomic and Peptidomic Approaches in Cancer Immunotherapy: Unveiling the Immune Microenvironment
The scope of this thematic issue centers on the integration of proteomic and peptidomic technologies into the field of cancer immunotherapy, with a particular emphasis on exploring the tumor immune microenvironment. This issue aims to gather contributions that illustrate the application of these advanced methodologies in unveiling the complex interplay ...read more
Artificial Intelligence for Protein Research
Protein research, essential for understanding biological processes and creating therapeutics, faces challenges due to the intricate nature of protein structures and functions. Traditional methods are limited in exploring the vast protein sequence space efficiently. Artificial intelligence (AI) and machine learning (ML) offer promising solutions by improving predictions and speeding up ...read more
Nutrition and Metabolism in Musculoskeletal Diseases
The musculoskeletal system consists mainly of cartilage, bone, muscles, tendons, connective tissue and ligaments. Balanced metabolism is of vital importance for the homeostasis of the musculoskeletal system. A series of musculoskeletal diseases (for example, sarcopenia, osteoporosis) are resulted from the dysregulated metabolism of the musculoskeletal system. Furthermore, metabolic diseases (such ...read more
Protein Folding, Aggregation and Liquid-Liquid Phase Separation
Protein folding, misfolding and aggregation remain one of the main problems of interdisciplinary science not only because many questions are still open, but also because they are important from the point of view of practical application. Protein aggregation and formation of fibrillar structures, for example, is a hallmark of a ...read more
Related Journals
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers
Related Articles
-
Machine Learning Approaches in Parkinson’s Disease
Current Medicinal Chemistry Targeting Epithelial-Mesenchymal Transition Phenotype for Gastro-Intestinal Cancer
Current Pharmaceutical Design The ATP-driven Hsp60 Machinery: Biological and Clinical Implications
Current Immunology Reviews (Discontinued) Role of the Dopamine Transporter in the Action of Psychostimulants, Nicotine, and Other Drugs of Abuse
CNS & Neurological Disorders - Drug Targets A Brief History of Davanloo’s Intensive Short-Term Dynamic Psychotherapy
Current Psychiatry Reviews Altered Functional Connectivity of the Marginal Division in Alzheimer’s Disease
Current Alzheimer Research Collagen: The Oldest Scaffold for Tissue Regeneration
Current Tissue Engineering (Discontinued) Computational Development of Selective nNOS Inhibitors: Binding Modes and Pharmacokinetic Considerations
Current Medicinal Chemistry Metabolic Cooperation in Testis as a Pharmacological Target: From Disease to Contraception
Current Molecular Pharmacology Drug Therapy in Brugada Syndrome
Current Drug Targets - Cardiovascular & Hematological Disorders Herbal Resources to Combat a Progressive & Degenerative Nervous System Disorder- Parkinson’s Disease
Current Drug Targets Poly(ADP-Ribose) Polymerase Inhibitors: New Pharmacological Functions and Potential Clinical Implications
Current Pharmaceutical Design Rational Drug Design Approach of Receptor Tyrosine Kinase Type III Inhibitors
Current Medicinal Chemistry The Seek of Neuroprotection: Introducing Cannabinoids
Recent Patents on CNS Drug Discovery (Discontinued) Molecular Modeling and Simulation of Membrane Lipid-Mediated Effects on GPCRs
Current Medicinal Chemistry Drug Delivery Across the Blood-Brain Barrier
Current Nanoscience Neural Stem Cell Niches in Health and Diseases
Current Pharmaceutical Design Adenylating Enzymes in Mycobacterium tuberculosis as Drug Targets
Current Topics in Medicinal Chemistry Potential of Bone Marrow Stromal Cells in Applications for Neuro-Degenerative, Neuro-Traumatic and Muscle Degenerative Diseases
Current Neuropharmacology Caffeine; the Forgotten Potential for Parkinson's Disease
CNS & Neurological Disorders - Drug Targets