Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions

Commonly used FRET fluorophores promote collapse of an otherwise disordered protein

(2019) Joshua A. Riback et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions

(2018) Alex S. Holehouse et al.   Annual Review of Biophysics

Saxs Confirms that FRET Dyes Promote Collapse of an Otherwise Fully Disordered Protein

(2018) Joshua A. Riback et al.   BIOPHYSICAL JOURNAL

Site-specific time-resolved FRET reveals local variations in the unfolding mechanism in an apparently two-state protein unfolding transition

(2018) Sandhya Bhatia et al.   PHYSICAL CHEMISTRY CHEMICAL PHYSICS

Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

(2018) Gustavo Fuertes et al.   SCIENCE

Response to Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

(2018) Joshua A. Riback et al.   SCIENCE

Comment on “Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water”

(2018) Robert B. Best et al.   SCIENCE

Collapse Precedes Folding in Denaturant-Dependent Assembly of Ubiquitin

(2017) Govardhan Reddy et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Monomeric Huntingtin Exon 1 Has Similar Overall Structural Features for Wild-Type and Pathological Polyglutamine Lengths

(2017) John B. Warner et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements

(2017) Gustavo Fuertes et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Innovative scattering analysis shows that hydrophobic disordered proteins are expanded in water

(2017) Joshua A. Riback et al.   SCIENCE

Protein collapse is encoded in the folded state architecture

(2017) Himadri S. Samanta et al.   Soft Matter

Single-Molecule FRET Spectroscopy and the Polymer Physics of Unfolded and Intrinsically Disordered Proteins

(2016) Benjamin Schuler et al.   Annual Review of Biophysics

Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment

(2016) Wenwei Zheng et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Consistent View of Polypeptide Chain Expansion in Chemical Denaturants from Multiple Experimental Methods

(2016) Alessandro Borgia et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation

(2016) Erik W. Martin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Cryptic sequence features within the disordered protein p27Kip1regulate cell cycle signaling

(2016) Rahul K. Das et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Comprehensive structural and dynamical view of an unfolded protein from the combination of single-molecule FRET, NMR, and SAXS

(2016) Mikayel Aznauryan et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Relating sequence encoded information to form and function of intrinsically disordered proteins

(2015) Rahul K Das et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins

(2015) Alexey G. Kikhney et al.   FEBS LETTERS

A Rigorous and Efficient Method To Reweight Very Large Conformational Ensembles Using Average Experimental Data and To Determine Their Relative Information Content

(2015) Hoi Tik Alvin Leung et al.   Journal of Chemical Theory and Computation

An Adequate Account of Excluded Volume Is Necessary To Infer Compactness and Asphericity of Disordered Proteins by Förster Resonance Energy Transfer

(2015) Jianhui Song et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Quantitative Assessments of the Distinct Contributions of Polypeptide Backbone Amides versus Side Chain Groups to Chain Expansion via Chemical Denaturation

(2015) Alex S. Holehouse et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability

(2015) Sagar V. Kathuria et al.   PROTEIN SCIENCE

Structural origin of slow diffusion in protein folding

(2015) H. S. Chung et al.   SCIENCE

Advanced ensemble modelling of flexible macromolecules using X-ray solution scattering

(2015) Giancarlo Tria et al.   IUCrJ

Single-Molecule Studies of Intrinsically Disordered Proteins

(2014) Marco Brucale et al.   CHEMICAL REVIEWS

Microsecond Barrier-Limited Chain Collapse Observed by Time-Resolved FRET and SAXS

(2014) Sagar V. Kathuria et al.   JOURNAL OF MOLECULAR BIOLOGY

Energetically significant networks of coupled interactions within an unfolded protein

(2014) J.-H. Cho et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Single-molecule spectroscopy reveals polymer effects of disordered proteins in crowded environments

(2014) Andrea Soranno et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Denatured State Ensembles with the Same Radii of Gyration Can Form Significantly Different Long-Range Contacts

(2013) Bowu Luan et al.   BIOCHEMISTRY

A quantitative measure for protein conformational heterogeneity

(2013) Nicholas Lyle et al.   JOURNAL OF CHEMICAL PHYSICS

Experiments and simulations show how long-range contacts can form in expanded unfolded proteins with negligible secondary structure

(2013) W. Meng et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Polypeptide chain collapse and protein folding

(2012) Jayant B. Udgaonkar   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Describing sequence–ensemble relationships for intrinsically disordered proteins

(2012) Albert H. Mao et al.   BIOCHEMICAL JOURNAL

The Amyloid State of Proteins in Human Diseases

(2012) David Eisenberg et al.   CELL

Small-Angle X-ray Scattering and Single-Molecule FRET Spectroscopy Produce Highly Divergent Views of the Low-Denaturant Unfolded State

(2012) Tae Yeon Yoo et al.   JOURNAL OF MOLECULAR BIOLOGY

Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy

(2012) A. Soranno et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy

(2012) H. Hofmann et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

The Protein-Folding Problem, 50 Years On

(2012) K. A. Dill et al.   SCIENCE

How, when and why proteins collapse: the relation to folding

(2011) Gilad Haran   CURRENT OPINION IN STRUCTURAL BIOLOGY

Microsecond Subdomain Folding in Dihydrofolate Reductase

(2011) Munehito Arai et al.   JOURNAL OF MOLECULAR BIOLOGY

How Fast-Folding Proteins Fold

(2011) K. Lindorff-Larsen et al.   SCIENCE

Proline-Rich Salivary Proteins Have Extended Conformations

(2010) Hélène Boze et al.   BIOPHYSICAL JOURNAL

The folding of single domain proteins—have we reached a consensus?

(2010) Tobin R Sosnick et al.   CURRENT OPINION IN STRUCTURAL BIOLOGY

Evidence for Initial Non-specific Polypeptide Chain Collapse During the Refolding of the SH3 Domain of PI3 Kinase

(2010) Amrita Dasgupta et al.   JOURNAL OF MOLECULAR BIOLOGY

Molecular Simulation ofab InitioProtein Folding for a Millisecond Folder NTL9(1−39)

(2010) Vincent A. Voelz et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Charge interactions can dominate the dimensions of intrinsically disordered proteins

(2010) S. Muller-Spath et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Non-native interactions play an effective role in protein folding dynamics

(2010) Patrícia F. N. Faísca et al.   PROTEIN SCIENCE

Probing Protein Folding Using Site-Specifically Encoded Unnatural Amino Acids as FRET Donors with Tryptophan

(2009) Shigeki J. Miyake-Stoner et al.   BIOCHEMISTRY

How accurate are polymer models in the analysis of Förster resonance energy transfer experiments on proteins?

(2009) Edward P. O’Brien et al.   JOURNAL OF CHEMICAL PHYSICS

The Limited Role of Nonnative Contacts in the Folding Pathways of a Lattice Protein

(2009) Brian C. Gin et al.   JOURNAL OF MOLECULAR BIOLOGY

Robust, high-throughput solution structural analyses by small angle X-ray scattering (SAXS)

(2009) Greg L Hura et al.   NATURE METHODS

Direct observation of barrier-limited folding of BBL by single-molecule fluorescence resonance energy transfer

(2009) F. Huang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Coordinate-dependent diffusion in protein folding

(2009) R. B. Best et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Small-Angle X-ray Scattering of Reduced Ribonuclease A: Effects of Solution Conditions and Comparisons with a Computational Model of Unfolded Proteins

(2008) Yuanyuan Wang et al.   JOURNAL OF MOLECULAR BIOLOGY

Role of Backbone−Solvent Interactions in Determining Conformational Equilibria of Intrinsically Disordered Proteins

(2008) Hoang T. Tran et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein

(2008) Y. Wu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Folding versus aggregation: Polypeptide conformations on competing pathways

(2007) Thomas R. Jahn et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS