scholarly article | Q13442814 |
P2093 | author name string | Marc S Wold | |
Gary W Daughdrill | |||
David F Lowry | |||
Pamela D Vise | |||
Katie E Olson | |||
Pranesh Narayanaswami | |||
P2860 | cites work | Non-globular domains in protein sequences: automated segmentation using complexity measures | Q36726009 |
Dissection of functional domains of the human DNA replication protein complex replication protein A. | Q36802969 | ||
Chemical shifts as a tool for structure determination | Q40576242 | ||
Structural flexibility of the linker region of human P-glycoprotein permits ATP hydrolysis and drug transport | Q42461714 | ||
Sequence-dependent correction of random coil NMR chemical shifts | Q43677693 | ||
Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. | Q44286601 | ||
The N-terminal prion domain of Ure2p converts from an unfolded to a thermally resistant conformation upon filament formation | Q44890766 | ||
Folding and binding | Q45178190 | ||
NMR nomenclature. Nuclear spin properties and conventions for chemical shifts (IUPAC Recommendations 2001) | Q55952105 | ||
Changes to the length of the flexible linker region of the Rieske protein impair the interaction of ubiquinol with the cytochromebc1complex | Q57828243 | ||
The Affinity-Enhancing Roles of Flexible Linkers in Two-Domain DNA-Binding Proteins† | Q58881325 | ||
Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA | Q24311910 | ||
Functional domains of the 70-kilodalton subunit of human replication protein A | Q24316316 | ||
NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain | Q24792064 | ||
Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker | Q27620027 | ||
1H, 13C and 15N chemical shift referencing in biomolecular NMR | Q27860609 | ||
Protein backbone angle restraints from searching a database for chemical shift and sequence homology | Q27861108 | ||
A hierarchy of SSB protomers in replication protein A. | Q27932319 | ||
Replication protein A: a heterotrimeric, single-stranded DNA-binding protein required for eukaryotic DNA metabolism | Q28245231 | ||
Relationship between nuclear magnetic resonance chemical shift and protein secondary structure | Q28252147 | ||
The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy | Q28293625 | ||
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease | Q29547582 | ||
Analysis of compositionally biased regions in sequence databases | Q29614389 | ||
Intrinsically unstructured proteins | Q29614784 | ||
Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm | Q29615865 | ||
Intrinsic disorder and protein function | Q29616415 | ||
Natively unfolded proteins: a point where biology waits for physics | Q29616416 | ||
Coupling of folding and binding for unstructured proteins | Q29616417 | ||
Coupling of local folding to site-specific binding of proteins to DNA | Q29616464 | ||
Calculation of ensembles of structures representing the unfolded state of an SH3 domain. | Q30168184 | ||
Spectral density function mapping using 15N relaxation data exclusively | Q30193137 | ||
Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView | Q30619296 | ||
Replication protein A interactions with DNA. 1. Functions of the DNA-binding and zinc-finger domains of the 70-kDa subunit | Q30668730 | ||
Replication protein A interactions with DNA. 2. Characterization of double-stranded DNA-binding/helix-destabilization activities and the role of the zinc-finger domain in DNA interactions | Q30668737 | ||
Replication protein A interactions with DNA. III. Molecular basis of recognition of damaged DNA. | Q30835547 | ||
The weak interdomain coupling observed in the 70 kDa subunit of human replication protein A is unaffected by ssDNA binding | Q30997034 | ||
Use of chemical shifts in macromolecular structure determination | Q34084326 | ||
Recognition between flexible protein molecules: induced and assisted folding | Q34141716 | ||
New methods of structure refinement for macromolecular structure determination by NMR. | Q34469265 | ||
What does it mean to be natively unfolded? | Q34488954 | ||
Oligomeric and polymeric aggregates formed by proteins containing expanded polyglutamine | Q34805750 | ||
Insights into the structure and dynamics of unfolded proteins from nuclear magnetic resonance | Q34989920 | ||
Intrinsically unstructured proteins evolve by repeat expansion | Q35206014 | ||
P433 | issue | 2 | |
P304 | page(s) | 113-124 | |
P577 | publication date | 2005-10-01 | |
P1433 | published in | Journal of Biomolecular Structure and Dynamics | Q15754747 |
P1476 | title | Secondary structure and dynamics of an intrinsically unstructured linker domain | |
P478 | volume | 23 |
Q43023020 | Computational studies reveal phosphorylation-dependent changes in the unstructured R domain of CFTR. |
Q43715232 | Dynamic behavior of an intrinsically unstructured linker domain is conserved in the face of negligible amino acid sequence conservation |
Q22061739 | Dynamic protein–DNA recognition: beyond what can be seen |
Q34197530 | Expanding the proteome: disordered and alternatively folded proteins |
Q34316593 | First principles calculations of thermodynamics and kinetic parameters and molecular dynamics simulations of acetylcholinesterase reactivators: can mouse data provide new insights into humans? |
Q44486815 | From protein sequence to dynamics and disorder with DynaMine |
Q22061730 | Fuzziness: linking regulation to protein dynamics |
Q38056343 | Mass spectrometry methods for intrinsically disordered proteins. |
Q33339291 | Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA) |
Q47602277 | Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins |
Search more.