scholarly article | Q13442814 |
P50 | author | Doug Barrick | Q62056400 |
P2093 | author name string | Ellen Kloss | |
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Spectroscopic Determination of Tryptophan and Tyrosine in Proteins* | Q29555850 | ||
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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding | Q29620340 | ||
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Local and long-range stability in tandemly arrayed tetratricopeptide repeats | Q33936836 | ||
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Predicting coupling limits from an experimentally determined energy landscape | Q35690994 | ||
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DNA mimicry by proteins and the control of enzymatic activity on DNA. | Q36525377 | ||
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Repeat-protein folding: new insights into origins of cooperativity, stability, and topology | Q36982772 | ||
An experimentally determined protein folding energy landscape | Q37557446 | ||
The leucine-rich repeat domain of Internalin B folds along a polarized N-terminal pathway | Q39132517 | ||
Stability of proteins: small globular proteins | Q39303667 | ||
Electrostatic stabilization of a thermophilic cold shock protein | Q39411179 | ||
Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues | Q40346399 | ||
Staphylococcal nuclease: a showcase of m-value effects | Q40539445 | ||
New PC versions of the kinetic-simulation and fitting programs, KINSIM and FITSIM | Q41576510 | ||
Charge-charge interactions influence the denatured state ensemble and contribute to protein stability | Q42026633 | ||
Folding thermodynamics and kinetics of the leucine-rich repeat domain of the virulence factor Internalin B | Q42162394 | ||
Structural characterization of the tumor suppressor p16, an ankyrin-like repeat protein | Q42845500 | ||
The effects of ionic strength on protein stability: the cold shock protein family | Q43030572 | ||
Studies of the Ankyrin Repeats of the Drosophila melanogaster Notch Receptor. 2. Solution Stability and Cooperativity of Unfolding | Q43809916 | ||
Electrostatic effects in highly charged proteins: salt sensitivity of pKa values of histidines in staphylococcal nuclease | Q43968663 | ||
Equilibrium folding and stability of myotrophin: a model ankyrin repeat protein | Q44038183 | ||
pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. | Q44670870 | ||
Experimental characterization of the folding kinetics of the notch ankyrin domain | Q46646140 | ||
Protein folding and stability using denaturants | Q46927993 | ||
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Side-chain effects on peptidyl-prolyl cis/trans isomerisation. | Q47923607 | ||
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A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range | Q52421063 | ||
Defective folding of mutant p16(INK4) proteins encoded by tumor-derived alleles | Q52522274 | ||
Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin | Q52894666 | ||
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Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. | Q54615581 | ||
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β-turns in proteins | Q67044372 | ||
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Fast-folding and slow-folding forms of unfolded proteins | Q69647574 | ||
Conformational stability and mechanism of folding of ribonuclease T1 | Q69652267 | ||
Ribonuclease T1 is stabilized by cation and anion binding | Q70394745 | ||
Nature of the charge distribution in proteins | Q70952678 | ||
Thermodynamic study of the acid denaturation of barnase and its dependence on ionic strength: evidence for residual electrostatic interactions in the acid/thermally denatured state | Q72076922 | ||
Hydrogen bonds and the pH dependence of ovomucoid third domain stability | Q72159564 | ||
pH dependence of stability of staphylococcal nuclease: evidence of substantial electrostatic interactions in the denatured state | Q73212774 | ||
The notch ankyrin domain folds via a discrete, centralized pathway | Q80100158 | ||
A new folding paradigm for repeat proteins | Q80392065 | ||
Application of the transfer model to understand how naturally occurring osmolytes affect protein stability | Q81309610 | ||
P433 | issue | 5 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | protein folding | Q847556 |
P304 | page(s) | 1195-1209 | |
P577 | publication date | 2008-09-04 | |
P1433 | published in | Journal of Molecular Biology | Q925779 |
P1476 | title | Thermodynamics, kinetics, and salt dependence of folding of YopM, a large leucine-rich repeat protein | |
P478 | volume | 383 |
Q30375581 | Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models |
Q41438086 | C-terminal deletion of leucine-rich repeats from YopM reveals a heterogeneous distribution of stability in a cooperatively folded protein |
Q33888074 | Consensus design of a NOD receptor leucine rich repeat domain with binding affinity for a muramyl dipeptide, a bacterial cell wall fragment |
Q27682510 | Crystal structure of an engineered YopM-InlB hybrid protein |
Q38672328 | Deletion of internal structured repeats increases the stability of a leucine-rich repeat protein, YopM |
Q41524471 | Diffuse transition state structure for the unfolding of a leucine-rich repeat protein. |
Q37129905 | Distribution and Evolution of Yersinia Leucine-Rich Repeat Proteins |
Q42687259 | Electrostatic Interactions and Protein Competition Reveal a Dynamic Surface in Gold Nanoparticle-Protein Adsorption |
Q35590129 | Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability |
Q28543085 | Probing conformational stability and dynamics of erythroid and nonerythroid spectrin: effects of urea and guanidine hydrochloride |
Q27679895 | Selection of Specific Protein Binders for Pre-Defined Targets from an Optimized Library of Artificial Helicoidal Repeat Proteins (alphaRep) |
Q44092783 | The Utilization of Competing Unfolding Pathways of Monellin Is Dictated by Enthalpic Barriers |
Q42733039 | Using Correlated Monte Carlo Sampling for Efficiently Solving the Linearized Poisson-Boltzmann Equation Over a Broad Range of Salt Concentration. |
Q41899145 | What have we learned from the studies of two-state folders, and what are the unanswered questions about two-state protein folding? |
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