288 research outputs found
Chapter 6 The Role of Corporate Governance in Macro-Prudential Regulation of Systemic Risk
Bank Regulation, Risk Management, and Compliance is a concise yet comprehensive treatment of the primary areas of US banking regulation – micro-prudential, macroprudential, financial consumer protection, and AML/CFT regulation – and their associated risk management and compliance systems. The book’s focus is the US, but its prolific use of standards published by the Basel Committee on Banking Supervision and frequent comparisons with UK and EU versions of US regulation offer a broad perspective on global bank regulation and expectations for internal governance. The book establishes a conceptual framework that helps readers to understand bank regulators’ expectations for the risk management and compliance functions. Informed by the author’s experience at a major credit rating agency in helping to design and implement a ratings compliance system, it explains how the banking business model, through credit extension and credit intermediation, creates the principal risks that regulation is designed to mitigate: credit, interest rate, market, and operational risk, and, more broadly, systemic risk. The book covers, in a single volume, the four areas of bank regulation and supervision and the associated regulatory expectations and firms’ governance systems. Readers desiring to study the subject in a unified manner have needed to separately consult specialized treatments of their areas of interest, resulting in a fragmented grasp of the subject matter. Banking regulation has a cohesive unity due in large part to national authorities’ agreement to follow global standards and to the homogenizing effects of the integrated global financial markets. The book is designed for legal, risk, and compliance banking professionals; students in law, business, and other finance-related graduate programs; and finance professionals generally who want a reference book on bank regulation, risk management, and compliance. It can serve both as a primer for entry-level finance professionals and as a reference guide for seasoned risk and compliance officials, senior management, and regulators and other policymakers. Although the book’s focus is bank regulation, its coverage of corporate governance, risk management, compliance, and management of conflicts of interest in financial institutions has broad application in other financial services sectors
Solvation vs. freezing in a heteropolymer globule
We address the response of a random heteropolymer to preferential solvation
of certain monomer types at the globule-solvent interface. For each set of
monomers that can comprise the molecule's surface, we represent the ensemble of
allowed configurations by a Gaussian distribution of energy levels, whose mean
and variance depend on the set's composition. Within such a random energy
model, mean surface composition is proportional to solvation strength under
most conditions. The breadth of this linear response regime arises from
approximate statistical independence of surface and volume energies. For a
diverse set of monomer types, the excess of solvophilic monomers at the surface
is large only for very strong solvent preference, even in the ground state.Comment: 10 pages, 1 figur
Redundancy, Unilateralism and Bias beyond GDP – results of a Global Index Benchmark
Eight out of ten leading international indices to assess developing countries in aspects beyond GDP are showing strong redundancy, bias and unilateralism. The quantitative comparison gives evidence for the fact that always the same countries lead the ranks with a low standard deviation.
The dependency of the GDP is striking: do the indices only measure indicators that are direct effects of a strong GDP?
While the impact of GDP can be discussed reverse as well, the standard deviation shows a strong bias: only one out of the twenty countries with the highest standard deviation is among the Top-20 countries of the world, but 11 countries among those with the lowest standard deviation.
Let’s have a look at the backsides of global statistics and methods to compare their findings.
The article is the result of a pre-study to assess Social Capital for development countries made for the German Federal Ministry for Economic Cooperation and Development. The study leaded to the UN Sustainable Development Goals (UN SDG) project World Social Capital Monitor
Redundancy, Unilateralism and Bias beyond GDP – results of a Global Index Benchmark
Eight out of ten leading international indices to assess developing countries in aspects beyond GDP are showing strong redundancy, bias and unilateralism. The quantitative comparison gives evidence for the fact that always the same countries lead the ranks with a low standard deviation.
The dependency of the GDP is striking: do the indices only measure indicators that are direct effects of a strong GDP?
While the impact of GDP can be discussed reverse as well, the standard deviation shows a strong bias: only one out of the twenty countries with the highest standard deviation is among the Top-20 countries of the world, but 11 countries among those with the lowest standard deviation.
Let’s have a look at the backsides of global statistics and methods to compare their findings.
The article is the result of a pre-study to assess Social Capital for development countries made for the German Federal Ministry for Economic Cooperation and Development. The study leaded to the UN Sustainable Development Goals (UN SDG) project World Social Capital Monitor
Heteropolymer Sequence Design and Preferential Solvation of Hydrophilic Monomers: One More Application of Random Energy Model
In this paper, we study the role of surface of the globule and the role of
interactions with the solvent for designed sequence heteropolymers using random
energy model (REM). We investigate the ground state energy and surface monomer
composition distribution. By comparing the freezing transition in random and
designed sequence heteropolymers, we discuss the effects of design. Based on
our results, we are able to show under which conditions solvation effect
improves the quality of sequence design. Finally, we study sequence space
entropy and discuss the number of available sequences as a function of imposed
requirements for the design quality
Freezing Transition of Random Heteropolymers Consisting of an Arbitrary Set of Monomers
Mean field replica theory is employed to analyze the freezing transition of
random heteropolymers comprised of an arbitrary number () of types of
monomers. Our formalism assumes that interactions are short range and
heterogeneity comes only from pairwise interactions, which are defined by an
arbitrary matrix. We show that, in general, there exists a
freezing transition from a random globule, in which the thermodynamic
equilibrium is comprised of an essentially infinite number polymer
conformations, to a frozen globule, in which equilibrium ensemble is dominated
by one or very few conformations. We also examine some special cases of
interaction matrices to analyze the relationship between the freezing
transition and the nature of interactions involved.Comment: 30 pages, 1 postscript figur
Thermodynamic stability of folded proteins against mutations
By balancing the average energy gap with its typical change due to mutations
for protein-like heteropolymers with M residues, we show that native states are
unstable to mutations on a scale M* ~ (lambda/sigma_mu)^(1/zeta_s), where
lambda is the dispersion in the interaction free energies and sigma_mu their
typical change. Theoretical bounds and numerical estimates (based on complete
enumeration on four lattices) of the instability exponent zeta_s are given. Our
analysis suggests that a limiting size of single-domain proteins should exist,
and leads to the prediction that small proteins are insensitive to random
mutations.Comment: 5 pages, 3 figures, to be published in Physical Review Letter
Free Energy Self-Averaging in Protein-Sized Random Heteropolymers
Current theories of heteropolymers are inherently macrpscopic, but are
applied to folding proteins which are only mesoscopic. In these theories, one
computes the averaged free energy over sequences, always assuming that it is
self-averaging -- a property well-established only if a system with quenched
disorder is macroscopic. By enumerating the states and energies of compact 18,
27, and 36mers on a simplified lattice model with an ensemble of random
sequences, we test the validity of the self-averaging approximation. We find
that fluctuations in the free energy between sequences are weak, and that
self-averaging is a valid approximation at the length scale of real proteins.
These results validate certain sequence design methods which can exponentially
speed up computational design and greatly simplify experimental realizations.Comment: 4 pages, 3 figure
Random walks in the space of conformations of toy proteins
Monte Carlo dynamics of the lattice 48 monomers toy protein is interpreted as
a random walk in an abstract (discrete) space of conformations. To test the
geometry of this space, we examine the return probability , which is the
probability to find the polymer in the native state after Monte Carlo
steps, provided that it starts from the native state at the initial moment.
Comparing computational data with the theoretical expressions for for
random walks in a variety of different spaces, we show that conformational
spaces of polymer loops may have non-trivial dimensions and exhibit negative
curvature characteristic of Lobachevskii (hyperbolic) geometry.Comment: 4 pages, 3 figure
Non-monotonic variation with salt concentration of the second virial coefficient in protein solutions
The osmotic virial coefficient of globular protein solutions is
calculated as a function of added salt concentration at fixed pH by computer
simulations of the ``primitive model''. The salt and counter-ions as well as a
discrete charge pattern on the protein surface are explicitly incorporated. For
parameters roughly corresponding to lysozyme, we find that first
decreases with added salt concentration up to a threshold concentration, then
increases to a maximum, and then decreases again upon further raising the ionic
strength. Our studies demonstrate that the existence of a discrete charge
pattern on the protein surface profoundly influences the effective interactions
and that non-linear Poisson Boltzmann and Derjaguin-Landau-Verwey-Overbeek
(DLVO) theory fail for large ionic strength. The observed non-monotonicity of
is compared to experiments. Implications for protein crystallization are
discussed.Comment: 43 pages, including 17 figure
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