Elucidating the folding problem of helical peptides using empirical parameters

NMR with Proteins and Nucleic Acids

Wüthrich, K. (1986) · Europhysics news · doi:10.1051/epn/19861701011 · Cited by 8,028

Statistical mechanics of chain molecules

Flory, P. J., & Volkenstein, M. V. (1969) · Biopolymers · doi:10.1002/bip.1969.360080514 · Cited by 6,449

NMR of Proteins and Nucleic Acids

(2006) · Royal Society of Chemistry eBooks · doi:10.1039/9781847555236-00336 · Cited by 5,874

Determination of the helix and β form of proteins in aqueous solution by circular dichroism

Chen, Y.-H., Yang, J. T., & Chau, K. H. (1974) · Biochemistry · doi:10.1021/bi00713a027 · Cited by 2,070

Theory of the Phase Transition between Helix and Random Coil in Polypeptide Chains

Zimm, B., & Bragg, J. K. (1959) · The Journal of Chemical Physics · doi:10.1063/1.1730390 · Cited by 1,801

Structure of ubiquitin refined at 1.8 A resolution.

Vijay-Kumar, S., Bugg, C., & Cook, W. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90679-6 · Cited by 1,636

Amino Acid Preferences for Specific Locations at the Ends of α Helices

Richardson, J. S., & Richardson, D. C. (1988) · Science · doi:10.1126/science.3381086 · Cited by 1,364

A Thermodynamic Scale for the Helix-Forming Tendencies of the Commonly Occurring Amino Acids

O’Neil, K. T., & DeGrado, W. F. (1990) · Science · doi:10.1126/science.2237415 · Cited by 1,186

Calculation of conformational ensembles from potentials of mena force

Sippl, M. J. (1990) · Journal of Molecular Biology · doi:10.1016/s0022-2836(05)80269-4 · Cited by 1,068

A Novel, Highly Stable Fold of the Immunoglobulin Binding Domain of Streptococcal Protein G

Gronenborn, A. M., Filpula, D. R., Essig, N. Z., Achari, A., Whitlow, M. D., Wingfield, P. T., & Clore, G. M. (1991) · Science · doi:10.1126/science.1871600 · Cited by 816

Efficient enumeration and visualization of helix-coil ensembles

Hughes, R. G., Zhao, S., Oas, T. G., & Schmidler, S. C. (2023) · Biophysical Journal · doi:10.1016/j.bpj.2023.12.021 · Cited by 4

Characterization of aBrg1 hypomorphic allele demonstrates that genetic and biochemical activity are tightly correlated

Chandler, R. L., Zhang, Y. E., Magnuson, T., & Bultman, S. J. (2013) · Epigenetics · doi:10.4161/epi.26879 · Cited by 4

Structural Basis of α-Catenin Recognition by EspB from Enterohaemorrhagic E. coli Based on Hybrid Strategy Using Low-Resolution Structural and Protein Dissection

Hamaguchi, M., Kamikubo, H., Suzuki, K. N., Hagihara, Y., Yanagihara, I., Sakata, I., Kataoka, M., & Hamada, D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0071618 · Cited by 4

On the choice of force fields for studying the molecular dynamics of ion peptides and their dimers

Danilkovich, A. V., Tikhonov, D. A., Sobolev, E. V., Shadrina, T. E., & Udovichenko, I. P. (2011) · Mathematical Biology and Bioinformatics · doi:10.17537/2011.6.53 · Cited by 4

Role of side-chain interactions on the formation of α -helices in model peptides

Mahmoudinobar, F., Dias, C. L., & Zangi, R. (2015) · Physical Review E · doi:10.1103/physreve.91.032710 · Cited by 4

Modulation of the aggregation of an amyloidogenic sequence by flanking-disordered region in the intrinsically disordered antigen merozoite surface protein 2

Zhang, W., Zhang, J., MacRaild, C. A., Norton, R. S., Anders, R. F., & Zhang, X. (2018) · European Biophysics Journal · doi:10.1007/s00249-018-1337-8 · Cited by 4

Simulation of the Positive Inotropic Peptide S100A1ct in Aqueous Environment by Gaussian Accelerated Molecular Dynamics.

Glaser, M., Bruce, N. J., Han, S. B., & Wade, R. (2021) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c00902 · Cited by 5

Switching an active site helix in dihydrofolate reductase reveals limits to subdomain modularity

Zhao, V. Y., Rodrigues, J. V., Lozovsky, E. R., Hartl, D. L., & Shakhnovich, E. I. (2021) · Biophysical Journal · doi:10.1016/j.bpj.2021.09.032 · Cited by 4

The B domain of protein A retains residual structures in 6 M guanidinium chloride as revealed by hydrogen/deuterium‐exchange NMR spectroscopy

Yanaka, S., Yagi‐Utsumi, M., Kato, K., & Kuwajima, K. (2023) · Protein Science · doi:10.1002/pro.4569 · Cited by 3

Potentiality of Weed Plants for Phytoremediation of Heavy Metal Polluted Soil

Bhayani, D., Siddhapura, S. P., Sindhav, S. R., & Jadeja, B. A. (2023) · International Journal of Environment and Climate Change · doi:10.9734/ijecc/2023/v13i51785 · Cited by 4

Larger Helical Populations in Peptides Derived from the Dimerization Helix of the Capsid Protein of HIV-1 Results in Peptide Binding toward Regions Other than the “Hotspot” Interface

Doménech, R., Bocanegra, R., González‐Muñiz, R., Gómez, J., Mateu, M. G., & Neira, J. L. (2011) · Biomacromolecules · doi:10.1021/bm2007168 · Cited by 4

Glutamine 53 is a gatekeeper residue in the FK506 binding protein.

Korepanova, A., Douglas, C., & Logan, T. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00943-9 · Cited by 4

Protein Design

Yennamalli, R. M. (2019) · Encyclopedia of Bioinformatics and Computational Biology · doi:10.1016/b978-0-12-809633-8.20151-9

Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints

Notari, E., Wood, C. W., & Michel, J. (2025) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c01695 · Cited by 4

ALS mutations disrupt self-association between the ubiquilin STI1 hydrophobic groove and internal placeholder sequences

Onwunma, J., Binsabaan, S., Allen, S. P., Thanthirige, S. R., Gaur, D., Sankaran, B., & Wohlever, M. L. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00745-9 · Cited by 10

Examination of the Effect of N‐terminal Diproline and Charged Side Chains on the Stabilization of Helical Conformation in Alanine–based Short Peptides: A Molecular Dynamics Study

Goyal, B., Srivastava, K. R., & Durani, S. (2016) · ChemistrySelect · doi:10.1002/slct.201601381 · Cited by 3

Prerequisites for Stabilizing Long-Range Synergistic Interactions among b-, c-, and f-Residues in Coiled Coils

Stern, K. L., Dalley, N. A., McMurray, N. T., Billings, W. M., Loftus, T. J., Jones, Z. B., Hadfield, J. R., & Price, J. L. (2022) · Biochemistry · doi:10.1021/acs.biochem.1c00760 · Cited by 3

Modulating long‐range energetics via helix stabilization: A case study using T4 lysozyme

Rosemond, S. N., Hamadani, K. M., Cate, J. H. D., & Marqusee, S. (2018) · Protein Science · doi:10.1002/pro.3521 · Cited by 3

Induced cytotoxicity of peptides by intracellular native chemical ligation

Lee, J., Oh, E., Lee, E., Park, H. J., & Kim, C. (2022) · New Journal of Chemistry · doi:10.1039/d2nj02053j · Cited by 3

Chain Sliding versus β‐Sheet Formation upon Shearing Single α‐Helical Coiled Coils

Tsirigoni, A., Goktas, M., Atris, Z., Valleriani, A., Verde, A. V., & Blank, K. G. (2023) · Macromolecular Bioscience · doi:10.1002/mabi.202200563 · Cited by 3

The N‐terminal intrinsically disordered region of Ncb5or docks with the cytochrome b 5 core to form a helical motif that is of ancient origin

Benson, D. R., Deng, B., Kashipathy, M. M., Lovell, S., Battaile, K. P., Cooper, A., Gao, P., Fenton, A. W., & Zhu, H. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26647 · Cited by 3

Substitution of a proline residue in the frog skin host-defense peptide, figainin-2PL by D-lysine generates an analog with potent activity against antibiotic-resistant ESKAPE pathogens

Guilhaudis, L., Cunning, T. S., Delaney, J. J., Ternan, N. G., Mechkarska, M., Attoub, S., & Conlon, J. M. (2025) · Peptides · doi:10.1016/j.peptides.2025.171430 · Cited by 3

Mechanische Verstärkung von Coiled Coils mit Lactam und Histidin‐Metall‐Klammern

López‐García, P., de Araujo, A. D., Bergues-Pupo, A. E., Tunn, I., Fairlie, D. P., & Blank, K. G. (2020) · Angewandte Chemie · doi:10.1002/ange.202006971 · Cited by 3

The helix nucleation site and propensity of the synthetic mitochondrial presequence of ornithine carbamoyltransferase.

de Jongh, H. D. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01654.x · Cited by 2

Molecular Simulations Find Stable Structures in Fragments of Protein G.

Urbič, T., Urbič, T., Avbelj, F., & Dill, K. A. (2008) · PubMed · Cited by 3

Deciphering the structural code for proteins: Helical propensities in domain classes and statistical multiresidue information in α‐helices

Negrete, J. A., Viñuales, Y., & Palau, J. (1998) · Protein Science · doi:10.1002/pro.5560070613 · Cited by 3

Diffusion–collision model algorithms for protein folding kinetics

Vasilkoski, Z., & Weaver, D. L. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20032 · Cited by 1

Intron-Encoded Domain of Herstatin, An Autoinhibitor of Human Epidermal Growth Factor Receptors, Is Intrinsically Disordered

Tashiro, D., Suetaka, S., Sato, N., Ooka, K., Kunihara, T., Kudo, H., Inatomi, J., Hayashi, Y., & Arai, M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.862910 · Cited by 3

Peptide fragment studies on the folding elements of dihydrofolate reductase from Escherichia coli

Arai, M., & Iwakura, M. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20675 · Cited by 3

Pairwise amino acid secondary structural propensities

Chemmama, I. E., Chapagain, P. P., & Gerstman, B. S. (2015) · Physical Review E · doi:10.1103/physreve.91.042709 · Cited by 3

Dual Self‐Promoted Ring‐Opening Polymerization towards Cationic Polypeptoids with Stable Helices

Gan, K., Zuckermann, R. N., Zhao, N., Xuan, S., & Zhang, Z. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202521129 · Cited by 2

The ‘Shape-Shifter’ Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences

Smith, L. J., Green, C. W., & Redfield, C. (2021) · Biomolecules · doi:10.3390/biom11050642 · Cited by 2

Influence of organization of native protein structure on its folding: Modeling of the folding of α-helical proteins

Glyakina, A. V., & Galzitskaya, O. V. (2010) · Biochemistry (Moscow) · doi:10.1134/s0006297910080079 · Cited by 2

Are the same or different amino acid residues responsible for correct and incorrect protein folding?

Galzitskaya, O. V. (2009) · Biochemistry (Moscow) · doi:10.1134/s0006297909020096 · Cited by 2

Structural and pharmacological characteristics of chimeric peptides derived from peptide E and beta-endorphin reveal the crucial role of the C-terminal YGGFL and YKKGE motifs in their analgesic properties.

Condamine, E., Courchay, K., Rego, J. D., Leprince, J., Mayer, C., Davoust, D., Costentin, J., & Vaudry, H. (2010) · Peptides · doi:10.1016/j.peptides.2010.01.012 · Cited by 4

Stabilities and Dynamics of Protein Folding Nuclei by Molecular Dynamics Simulation*

Song, Y., Zhou, X., Zheng, W., & Wang, Y. (2017) · Communications in Theoretical Physics · doi:10.1088/0253-6102/68/1/137 · Cited by 2

Induced cytotoxicity of peptides with crypto-thioester through native chemical ligation

Lee, J., Oh, E., Kim, J. H., Kim, K., Park, H. J., & Kim, C. (2023) · New Journal of Chemistry · doi:10.1039/d2nj05037d · Cited by 2

Purification, conformational analysis and cytotoxic activities of host-defense peptides from the Tungara frog Engystomops pustulosus (Leptodactylidae; Leiuperinae)

Conlon, J. M., Guilhaudis, L., Attoub, S., Coquet, L., Leprince, J., Jouenne, T., & Mechkarska, M. (2023) · Amino Acids · doi:10.1007/s00726-023-03312-2 · Cited by 2

Evaluation of the antiviral activity of new dermaseptin analogs against Zika virus

Haddad, H., Tangy, F., Ouahchi, I., SAHTOUT, W., Ouni, B., & Zaïri, A. (2024) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2024.101747 · Cited by 2

Chimeric dihydrofolate reductases display properties of modularity and biophysical diversity

Rodrigues, J., Ogbunugafor, C. B., Hartl, D. L., & Shakhnovich, E. (2019) · Protein Science · doi:10.1002/pro.3646 · Cited by 2

PESCADOR: The PEptides in Solution ConformAtion Database: Online Resource

Pajon, A., Vranken, W., Jiménez, M., Rico, M., & Wodak, S. (2002) · Journal of Biomolecular NMR · doi:10.1023/a:1016346127093 · Cited by 2

Structural polymorphism of coiled‐coils from the stalk domain of SARS‐CoV‐2 spike protein

Živič, Z., Strmšek, Ž., Novinec, M., Lah, J., & Hadži, S. (2022) · The FASEB Journal · doi:10.1096/fj.202101670r · Cited by 2

A data base of minimally frustrated alpha helical segments extracted from proteins according to an entropy criterion.

Casadio, R., Compiani, M., Fariselli, P., & Martelli, P. L. (1999) · PubMed · Cited by 2

Application of multiple sequence alignment profiles to improve protein secondary structure prediction

Cuff, J. A., & Barton, G. J. (2000) · Proteins Structure Function and Bioinformatics · doi:10.1002/1097-0134(20000815)40:3 · Cited by 773

A minor β‐structured conformation is the active state of a fusion peptide of vesicular stomatitis virus glycoprotein

Sarzedas, C. G., Lima, C. S., Juliano, M., Juliano, L., Valente, A., Poian, A. D. D., & Almeida, F. (2008) · Journal of Peptide Science · doi:10.1002/psc.934 · Cited by 1

Structural and thermodynamic encoding in the sequence of rat microsomal cytochrome b5

Lecomte, J. T. J., Mukhopadhyay, K., & Pond, M. P. (2007) · Biopolymers · doi:10.1002/bip.20892 · Cited by 2

Electrostatic contacts in the activator protein‐1 coiled coil enhance stability predominantly by decreasing the unfolding rate

Mason, J. (2009) · The FEBS Journal · doi:10.1111/j.1742-4658.2009.07440.x · Cited by 4

Design of Emulsification Peptides

Sheehan, D., Carey, K., & O’Sullivan, S. (1998) · Advances in food and nutrition research · doi:10.1016/s1043-4526(08)60094-7 · Cited by 2

Antimicrobial peptides and the interplay between microbes and host : towards preventing porcine infections with Streptococcus suis

Gaiser, R. A. (2016) · doi:10.18174/387767 · Cited by 2

The N-terminal intrinsically disordered region of Ncb5or docks with the cytochrome b5 core to form a helical motif that is of ancient originPreprint

Zhu, H., Benson, D. R., Deng, B., Kashipathy, M. M., Lovell, S., Battaile, K. P., Cooper, A., Gao, P., & Fenton, A. W. (2023) · doi:10.22541/au.169002203.35444701/v1 · Cited by 2

Molecular switching in transcription through splicing and proline-isomerization regulates stress responses in plantsPreprint

Theisen, F. F., Prestel, A., Elkjær, S., Leurs, Y. H. A., Morffy, N., Strader, L. C., O’Shea, C., Teilum, K., Kragelund, B. B., & Skriver, K. (2023) · Research Square · doi:10.21203/rs.3.rs-3034274/v1 · Cited by 2

Electrostatic origin of a stabilizing synergistic interaction among b‐, c‐, and f‐residues in a trimeric coiled coil

Dalley, N. A., Stern, K. L., Kitchen, R. R., Lloyd, K. B., & Price, J. L. (2023) · Peptide Science · doi:10.1002/pep2.24336 · Cited by 1

In vitro Antileishmanial Activity and In silico Molecular Modeling Studies of Novel Analogs of Dermaseptins S4 and B2

Haddad, H., Rodrigues, K. A. D. F., Othman, H., Véras, L. M. C., Rodrigues, R. R. L., Ouahchi, I., Ouni, B., & Zaïri, A. (2024) · Current Pharmaceutical Biotechnology · doi:10.2174/0113892010296038240427050421 · Cited by 1

Rationally designed, ACE2 mimetic binder to the SARS Cov-2 associated Spike protein for COVID-19 therapeutics and beyond

Peters, M. H., & Pei, X. Y. (2025) · Scientific Reports · doi:10.1038/s41598-025-21023-4 · Cited by 1

Antibacterial activity of peptide derivatives of dermaseptins against multidrug-resistant Klebsiella pneumoniae and Staphylococcus epidermis

Haddad, H., Al‐Rashidi, R. R., Loghmari, A., SAHTOUT, W., Boukadida, R., Dahmene, R., Ettouil, E., Othman, H., Ouahchi, I., & Zaïri, A. (2026) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2026.102449 · Cited by 1

ABSEIL: A Polypeptide Helicity and Ensemble Prediction Tool.

Hortman, H., Zhang, R.-L., Hughes, R. G., Castillo, M., Chen, E., Evans, S., Ortega, J., Bandini, J., McCahill, M., Schmidler, S. C., et al. (2026) · Journal of Molecular Biology · doi:10.1016/j.jmb.2026.169675 · Cited by 2

NMR Analysis of the Interactions and Conformational Plasticity of Dynein Intermediate Chain

Jara, K. A., & Barbar, E. J. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-2958-1_15 · Cited by 1

Activatable anticancer peptides with mutually suppressed bioactivity and their induced cytotoxicity by matrix metalloproteinase-2

Lee, J., Kim, H. G., & Oh, E. (2024) · New Journal of Chemistry · doi:10.1039/d4nj03404j · Cited by 1

Dissecting the Roles of Electrostatic Interactions in Modulating the Folding Stability and Cooperativity of Engrailed Homeodomain

Xu, C., & Chu, X. (2024) · Biochemistry · doi:10.1021/acs.biochem.4c00645 · Cited by 1

Large Protein Folding and Dynamics Studied by Advanced Hydrogen Exchange Methods

Walters, B. T. (2013) · Scholarly Commons (University of Pennsylvania) · Cited by 1

Unveiling the folding mechanism of the Bromodomains

Petrosino, M., Bonetti, D., Pasquo, A., Lori, L., Chiaraluce, R., Consalvi, V., & Travaglini‐Allocatelli, C. (2017) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2017.06.009 · Cited by 1

Self-consistent field approach to protein structure and stability

Dimitrov, R. (1999) · doi:10.18174/196195 · Cited by 1

Design and Stability of α‐Helices

Doig, A. J., Errington, N., & Iqbalsyah, T. M. (2008) · Protein Science Encyclopedia · doi:10.1002/9783527610754.ed06 · Cited by 1

Secondary Structure as a Conformational Determinant in Processing of Peptide Precursors at Dibasic Amino Acids

Lazar, N., Brakch, N., Panchal, M., Cohen, P., & Rholam, M. (2003) · Journal of Spectroscopy · doi:10.1155/2003/819640 · Cited by 1

Synthetic peptides mimicking the interleukin‐6/gp 130 interaction: a two‐helix bundle system. Design and conformational studies

Zaccaro, L., Bucci, E., Vitale, R., Perretta, G., Fattorusso, R., Benedetti, E., Saviano, M., & Pedone, C. (2003) · Journal of Peptide Science · doi:10.1002/psc.434 · Cited by 2

The Chemical Shift Index method applied to resin‐bound peptides

Fruchart, J.-S., Lippens, G. M., Warrassꝉ, R., Seetharaman, C., Dhalluin, C., & Boutillon, C. (2000) · Journal of Peptide Research · doi:10.1034/j.1399-3011.2000.00753.x · Cited by 1

Protein engineering to explore and improve affinity ligands

Linhult, M. (2003) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 1

Prediction of Factors Determining Changes in Stability in Protein Mutants

Parthiban, V. (2006) · Kölner Universitäts PublikationsServer (Universität zu Köln) · Cited by 1

UNDERSTANDING FORCES THAT CONTRIBUTE TO PROTEIN STABILITY: APPLICATION FOR INCREASING PROTEIN STABILITY

Fu, H. (2009) · OakTrust (Texas A&M University Libraries) · Cited by 1

Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in the activation domain of a transcription factorPreprint

Escobedo, A., Topal, B., Kunze, M. B. A., Aranda, J., Chiesa, G., Mungianu, D., Bernardo‐Seisdedos, G., Eftekharzadeh, B., Gairí, M., Pierattelli, R., et al. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/447896 · Cited by 2

The nature of the α-helix

(1994) · Nature Structural & Molecular Biology · doi:10.1038/nsb0694-343 · Cited by 1

Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clock

(2022) · doi:10.1101/2022.11.03.515097 · Cited by 1

Phosphorylation, disorder, and phase separation govern the behavior of Frequency in the fungal circadian clockPreprint

Tariq, D., Maurici, N., Bartholomai, B. M., Chandrasekaran, S., Dunlap, J., Bah, A., & Crane, B. R. (2024) · eLife · doi:10.7554/elife.90259.2 · Cited by 1

An Extremely Versatile Polyglutamate Alignment Medium to Measure Residual Dipolar Couplings in non-Polar and Polar SolventsPreprint

Laux, L., Alcaraz-Janßen, M., & Thiele, C. M. (2025) · ChemRxiv · doi:10.26434/chemrxiv-2025-808gp · Cited by 1

Direct computation of long time processes in peptides and proteins: Reaction path study of the coil-to-helix transition in polyalanine

Huo, S., & Straub, J. E. (1999) · Proteins Structure Function and Bioinformatics · doi:10.1002/(sici)1097-0134(19990801)36:2 · Cited by 50

STABILIZING INTERACTIONS IN THE H2A-H2B MONOMERIC AND DIMERIC KINETIC INTERMEDIATES

Guyett, P. J. (2011) · Research Exchange (Washington State University)

Identification of a conserved cluster in the RH domain of GRK critical for activation by GPCRs

Baameur, F. (2009) · Digital Commons-TMC (Texas Medical Center)

Charge‐Induced Effects on Acid–Base Titration and Conformational Stability of Proteins and Polypeptides

Hermans, J. (2012) · doi:10.1002/9781118165850.ch12

Navigating the Extremes of Biological Datasets for Reliable Structural Inference and Design

Hannigan, B. T. (2013) · ScholarlyCommons (University of Pennsylvania)

Conformational dynamics and stability of structured peptides and small proteins

Reiner, A. (2009) · edoc (University of Basel) · doi:10.5451/unibas-004761466

Helix–Coil Transition

Aloy, P. (2004) · Dictionary of Bioinformatics and Computational Biology · doi:10.1002/0471650129.dob0315

Predicting Free Energy Changes of Mutations in Proteins

Guérois, R., Mendes, J., & Serrano, L. G. (2008) · Wiley eBooks · doi:10.1002/9783527610754.sf02

SPEKTROSKOPISCHE STRUKTURANALYTIK SYNTHETISCHER POLYPEPTIDE

Petry, R. (2002) · Online Publication Service of Würzburg University (Würzburg University)

Protein Folding: Energetics

Baldwin, R. L. (2008) · Wiley Encyclopedia of Chemical Biology · doi:10.1002/9780470048672.wecb482

Dissecting Key Determinants for Calcium and Calmodulin Regulation of GAP Junction and Viral Protein

Chen, Y. (2022) · Digital Archive @ GSU · doi:10.57709/2791701

CropGen-making the case for crop biotechnology

Moses, V. (2000) · Pesticide Outlook · doi:10.1039/b006364i

Análisis estructural y conformacional de E6*I, un producto de procesamiento alternativo derivado de la oncoproteína E6 de HPV16

Heer, A. (2012) · Repositorio Digital Institucional de la Universidad de Buenos Aires (Universidad de Buenos Aires)

Fragmentos de tropomiosina - estudos da estabilidade conformacional e da interação cabeça-cauda

Paulucci-Holthauzen, A. A. (2018) · doi:10.11606/t.46.2018.tde-23042018-114148

Structural Characterization of Disordered States of Proteins

Marsh, J. A. (2010) · TSpace (University of Toronto)

NMR Studies of SH3 Domain Structure and Function

Bezsonova, I. (2009) · TSpace (University of Toronto)

Antimicrobial peptides with therapeutic potential from skin secretions of polyploid frogs of the Pipidae family

Mechkarska, M. (2013) · doi:10.18174/255770

Design, Synthesis, and Experimental Validation of Peptide Ligands Targeting Mycobacterium tuberculosis σ Factors.

Vishwanath, S., Banerjee, S., Jamithireddy, A., Srinivasan, N., Gopal, B., & Chatterjee, J. (2017) · Biochemistry · doi:10.1021/acs.biochem.6b01267

Estabilidad, plegamiento y asociación del dominio de dimerización de la proteína de la cápsida del virus de la inmunodeficiencia humana

Moya, L., & del Carmen, M. (2005)

Folding of protein secondary structures using a novel polarizable force field method

Yip, Y. M. (2017) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/72948

Disorder Levels of c-Myb Transactivation Domain Regulate its Binding Affinity to the KIX Domain of CREB Binding Protein

Poosapati, A. (2017) · Digital Commons - University of South Florida (University of South Florida)

On The Choice of Force Fields for Studying the Molecular Dynamics of Ion Peptides and Their Dimers

Danilkovich, A. V., Tikhonov, D. A., Sobolev, E. V., Shadrina, T. E., & Udovichenko, I. P. (2018) · Mathematical Biology and Bioinformatics · doi:10.17537/2018.13.t29

Hydrogenosomal tail-anchored proteins are targeted to both mitochondria and ER upon their expression in yeast cells

Ferdigg, A., Dimmer, K., Rapaport, D., & Vitali, D. G. (2020) · PLoS ONE · doi:10.1371/journal.pone.0237982

Amyloid proteins and fibrils stability

Mahmoudinobar, F. (2019)

HSymM-guided engineering of the immunodominant p53 transactivation domain putative peptide antigen for improved binding to its anti-p53 monoclonal antibody

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Predicting Free Energy Changes of Mutations in Proteins

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Qualitative and quantitative analysis of the secondary structure of cytochrome C Langmuir-Blodgett films

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Structure, stability and folding of the α-helix

Doig, A. J., Andrew, C. D., Cochran, D. A. E., Hughes, E., Penel, S., Sun, J. K., Stapley, B. J., Clarke, D. T., & Jones, G. R. (2001) · Biochemical Society Symposia · doi:10.1042/bss0680095 · Cited by 13

Structure and Stability of the alpha-Helix. Lessons for Design

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